DB code: M00205

CATH domain 1.-.-.- :
1.10.395.10 :
3.90.244.10 : Catalytic domain
3.90.188.10 : Catalytic domain
-.-.-.- :
1.10.620.20 : Ribonucleotide Reductase, subunit A Catalytic domain
E.C. 1.17.4.1
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
1.10.620.20 : Ribonucleotide Reductase, subunit A S00028 M00151 M00204
3.90.188.10 : M00204
3.90.244.10 : M00204

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P21524 Ribonucleoside-diphosphate reductase large chain 1
EC 1.17.4.1
Ribonucleotide reductase R1 subunit 1
Ribonucleotide reductase large subunit 1
NP_010993.1 (Protein)
NM_001178961.1 (DNA/RNA sequence)
PF03477 (ATP-cone)
PF02867 (Ribonuc_red_lgC)
PF00317 (Ribonuc_red_lgN)
[Graphical View]
P21672 Ribonucleoside-diphosphate reductase large chain 2
EC 1.17.4.1
Ribonucleotide reductase DNA damage-inducible regulatory subunit 2
Ribonucleotide reductase R1 subunit 2
Ribonucleotide reductase large subunit 2
NP_012198.3 (Protein)
NM_001179416.3 (DNA/RNA sequence)
PF03477 (ATP-cone)
PF02867 (Ribonuc_red_lgC)
PF00317 (Ribonuc_red_lgN)
[Graphical View]
P09938 Ribonucleoside-diphosphate reductase small chain 1
EC 1.17.4.1
Ribonucleotide reductase R2 subunit 1
Ribonucleotide reductase small subunit 1
NP_012508.1 (Protein)
NM_001181460.1 (DNA/RNA sequence)
PF00268 (Ribonuc_red_sm)
[Graphical View]
P49723 Ribonucleoside-diphosphate reductase small chain 2
EC 1.17.4.1
Ribonucleotide reductase R2 subunit 2
Ribonucleotide reductase small subunit 2
NP_011696.3 (Protein)
NM_001181309.3 (DNA/RNA sequence)
PF00268 (Ribonuc_red_sm)
[Graphical View]

KEGG enzyme name
ribonucleoside-diphosphate reductase
ribonucleotide reductase
CDP reductase
ribonucleoside diphosphate reductase
UDP reductase
ADP reductase
nucleoside diphosphate reductase
ribonucleoside 5'-diphosphate reductase
ribonucleotide diphosphate reductase
2'-deoxyribonucleoside-diphosphate:oxidized-thioredoxin2'-oxidoreductase
RR

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P21524 RIR1_YEAST 2''-deoxyribonucleoside diphosphate + thioredoxin disulfide + H(2)O = ribonucleoside diphosphate + thioredoxin. Heterotetramer of two large (R1) and two small (R2) subunits. S.cerevisiae has two different R1 subunits (RNR1 and RNR3) and two different R2 subunits (RNR2 and RNR4). The functional form of the small subunits is a RNR2-RNR4 heterodimer, where RNR2 provides the iron-radical center and RNR4 is required for proper folding of RNR2 and assembly with the large subunits. Under normal growth conditions, the active form of the large subunits is a homodimer of the constitutively expressed RNR1. In damaged cells or cells arrested for DNA synthesis, the reductase consists of multiple species because of the association of the small subunits (RNR2-RNR4) with either the RNR1 homodimer or a heterodimer of RNR1 and the damage-inducible RNR3. RNR1 interacts with the ribonucleotide reductase inhibitor SML1. Cytoplasm.
P21672 RIR3_YEAST 2''-deoxyribonucleoside diphosphate + thioredoxin disulfide + H(2)O = ribonucleoside diphosphate + thioredoxin. Heterotetramer of two large (R1) and two small (R2) subunits. S.cerevisiae has two different R1 subunits (RNR1 and RNR3) and two different R2 subunits (RNR2 and RNR4). The functional form of the small subunits is a RNR2-RNR4 heterodimer, where RNR2 provides the iron-radical center and RNR4 is required for proper folding of RNR2 and assembly with the large subunits. Under normal growth conditions, the active form of the large subunits is a homodimer of the constitutively expressed RNR1. In damaged cells or cells arrested for DNA synthesis, the reductase consists of multiple species because of the association of the small subunits (RNR2-RNR4) with either the RNR1 homodimer or a heterodimer of RNR1 and the damage-inducible RNR3. Cytoplasm.
P09938 RIR2_YEAST 2''-deoxyribonucleoside diphosphate + thioredoxin disulfide + H(2)O = ribonucleoside diphosphate + thioredoxin. Heterotetramer of two large (R1) and two small (R2) subunits. S.cerevisiae has two different R1 subunits (RNR1 and RNR3) and two different R2 subunits (RNR2 and RNR4). The functional form of the small subunits is a RNR2-RNR4 heterodimer, where RNR2 provides the iron-radical center and RNR4 is required for proper folding of RNR2 and assembly with the large subunits. Under normal growth conditions, the active form of the large subunits is a homodimer of the constitutively expressed RNR1. In damaged cells or cells arrested for DNA synthesis, the reductase consists of multiple species because of the association of the small subunits (RNR2-RNR4) with either the RNR1 homodimer or a heterodimer of RNR1 and the damage-inducible RNR3. Nucleus. Note=Found predominantly in the nucleus under normal growth conditions and is redistributed to the cytoplasm in damaged cells in a DNA replication and damage checkpoint-dependent manner. Binds 2 iron ions per subunit.
P49723 RIR4_YEAST 2''-deoxyribonucleoside diphosphate + thioredoxin disulfide + H(2)O = ribonucleoside diphosphate + thioredoxin. Heterotetramer of two large (R1) and two small (R2) subunits. S.cerevisiae has two different R1 subunits (RNR1 and RNR3) and two different R2 subunits (RNR2 and RNR4). The functional form of the small subunits is a RNR2-RNR4 heterodimer, where RNR2 provides the iron-radical center and RNR4 is required for proper folding of RNR2 and assembly with the large subunits. Under normal growth conditions, the active form of the large subunits is a homodimer of the constitutively expressed RNR1. In damaged cells or cells arrested for DNA synthesis, the reductase consists of multiple species because of the association of the small subunits (RNR2-RNR4) with either the RNR1 homodimer or a heterodimer of RNR1 and the damage-inducible RNR3. Nucleus. Note=Found predominantly in the nucleus under normal growth conditions and is redistributed to the cytoplasm in damaged cells in a DNA replication and damage checkpoint-dependent manner.

KEGG Pathways
Map code Pathways E.C.
MAP00230 Purine metabolism
MAP00240 Pyrimidine metabolism
MAP00480 Glutathione metabolism

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00023 C00002 C00342 C03723 C04232 C00343 C00001
E.C.
Compound Iron ATP Reduced thioredoxin Ribonucleoside diphosphate 2'-Deoxyribonucleoside diphosphate Oxidized thioredoxin H2O
Type heavy metal amine group,nucleotide amide group,carbohydrate,peptide/protein,sulfhydryl group nucleotide nucleotide amide group,carbohydrate,disulfide bond,peptide/protein H2O
ChEBI 18248
82664
15422
15377
PubChem 23925
5957
22247451
962
1zyzA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1zyzB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2cvsA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2cvtA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2cvxA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1zyzA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1zyzB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1zzdA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2cvsA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2cvtA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2cvuA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2cvvA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2cvwA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2cvxA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2cvyA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2eudA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1zyzA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1zyzB03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1zzdA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2cvsA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2cvtA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2cvuA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Bound:CDP Unbound Unbound
2cvvA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Bound:UDP Unbound Unbound
2cvwA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Bound:GDP Unbound Unbound
2cvxA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Bound:ADP Unbound Unbound
2cvyA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2eudA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Analogue:GCQ Unbound Unbound
1zyzA04 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1zyzB04 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1zzdA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2cvsA04 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2cvtA04 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:ANP Unbound Unbound Unbound Unbound
2cvuA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:ANP Unbound Unbound Unbound Unbound
2cvvA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:ANP Unbound Unbound Unbound Unbound
2cvwA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:TTP Unbound Unbound Unbound Unbound
2cvxA04 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:DGT Unbound Unbound Unbound Unbound
2cvyA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:TTP Unbound Unbound Unbound Unbound
2eudA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:ANP Unbound Unbound Unbound Unbound
1jk0A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:_ZN Unbound Unbound Unbound Unbound Unbound
1smqA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1smqB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1smqC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1smqD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1jk0B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1smsA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1smsB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
PDB;2r1r, 3r1r & Swiss-prot;P00452 & literature [14]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1zyzA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1zyzB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2cvsA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2cvtA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2cvxA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1zyzA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1zyzB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1zzdA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2cvsA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2cvtA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2cvuA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2cvvA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2cvwA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2cvxA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2cvyA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2eudA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1zyzA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 741;TYR 742
1zyzB03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 741;TYR 742
1zzdA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 741;TYR 742
2cvsA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 741;TYR 742
2cvtA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 741;TYR 742
2cvuA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 741;TYR 742
2cvvA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 741;TYR 742
2cvwA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 741;TYR 742
2cvxA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 741;TYR 742
2cvyA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 741;TYR 742
2eudA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 741;TYR 742
1zyzA04 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 218;ASN 426;CYS 428;GLU 430;CYS 443
1zyzB04 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 218;ASN 426;CYS 428;GLU 430;CYS 443
1zzdA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 218;ASN 426;CYS 428;GLU 430;CYS 443 disulfide bonded/oxidized form C218-C443
2cvsA04 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 218;ASN 426;CYS 428;GLU 430;CYS 443 disulfide bonded/oxidized form C218-C443
2cvtA04 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 218;ASN 426;CYS 428;GLU 430;CYS 443
2cvuA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 218;ASN 426;CYS 428;GLU 430;CYS 443
2cvvA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 218;ASN 426;CYS 428;GLU 430;CYS 443
2cvwA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 218;ASN 426;CYS 428;GLU 430;CYS 443
2cvxA04 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 218;ASN 426;CYS 428;GLU 430;CYS 443
2cvyA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 218;ASN 426;CYS 428;GLU 430;CYS 443 disulfide bonded/oxidized form C218-C443
2eudA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 218;ASN 426;CYS 428;GLU 430;CYS 443
1jk0A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 183 ASP 145;HIS 179(Iron-1);GLU 239;HIS 276(Iron-2);GLU 176;GLU 273(both Iron-1 & Iron-2)
1smqA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 183 ;HIS 179(Iron-1);GLU 239;HIS 276(Iron-2);GLU 176;GLU 273(both Iron-1 & Iron-2) invisible 145-149
1smqB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 183 ;HIS 179(Iron-1);GLU 239;HIS 276(Iron-2);GLU 176;GLU 273(both Iron-1 & Iron-2) invisible 145-149
1smqC Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 183 ;HIS 179(Iron-1);GLU 239;HIS 276(Iron-2);GLU 176;GLU 273(both Iron-1 & Iron-2) invisible 145-149
1smqD Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 183 ;HIS 179(Iron-1);GLU 239;HIS 276(Iron-2);GLU 176;GLU 273(both Iron-1 & Iron-2) invisible 145-149
1jk0B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 131
1smsA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 131
1smsB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 131

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[3]
Scheme I, p.12750
[3]
Scheme II, p.12750
[3]
Scheme III, p.12751
[7]
FIG. 4c, p.537
[9]
Scheme 1, p.8382
[9]
Scheme 2, p.8389
[9]
Scheme 3, p.8389
[9]
Scheme 4, p.8389
[10]
FScheme 2, p.10066
[13]
FIG. 2, p.31534
[14]
Figure 9, p.1088
[23]
SCHEME 1, p.60
[25]
SCHEME 1, p.5750
[25]
SCHEME 2, p.5752
[26]
Figure 3, p.313
[26]
Figure 4, p.314
[26]
Figure 7, p.316

References
[1]
Resource
Comments Subunit R2
Medline ID
PubMed ID 1963165
Journal Free Radic Res Commun
Year 1990
Volume 10
Pages 281-6
Authors Harder J, Follmann H
Title Identification of a free radical and oxygen dependence of ribonucleotide reductase in yeast.
Related PDB
Related UniProtKB
[2]
Resource
Comments Subunit R1
Medline ID
PubMed ID 11074005
Journal Mol Cell Biol
Year 2000
Volume 20
Pages 9076-83
Authors Zhao X, Georgieva B, Chabes A, Domkin V, Ippel JH, Schleucher J, Wijmenga S, Thelander L, Rothstein R
Title Mutational and structural analyses of the ribonucleotide reductase inhibitor Sml1 define its Rnr1 interaction domain whose inactivation allows suppression of mec1 and rad53 lethality.
Related PDB
Related UniProtKB
[3]
Resource
Comments Subunit R2
Medline ID
PubMed ID 11472128
Journal J Am Chem Soc
Year 2001
Volume 123
Pages 3569-76
Authors Bar G, Bennati M, Nguyen HH, Ge J, Stubbe JA, Griffin RG
Title High-frequency (140-GHz) time domain EPR and ENDOR spectroscopy: the tyrosyl radical-diiron cofactor in ribonucleotide reductase from yeast.
Related PDB
Related UniProtKB
[4]
Resource
Comments X-ray crystallography, Subunit R2
Medline ID
PubMed ID 11526233
Journal Proc Natl Acad Sci U S A
Year 2001
Volume 98
Pages 10073-8
Authors Voegtli WC, Ge J, Perlstein DL, Stubbe J, Rosenzweig AC
Title Structure of the yeast ribonucleotide reductase Y2Y4 heterodimer.
Related PDB 1jk0
Related UniProtKB
[5]
Resource
Comments X-ray crystallography, Subunit R2
Medline ID
PubMed ID 15196016
Journal Biochemistry
Year 2004
Volume 43
Pages 7736-42
Authors Sommerhalter M, Voegtli WC, Perlstein DL, Ge J, Stubbe J, Rosenzweig AC
Title Structures of the yeast ribonucleotide reductase Rnr2 and Rnr4 homodimers.
Related PDB 1smq 1sms
Related UniProtKB
[6]
Resource
Comments Subunit R1
Medline ID
PubMed ID 16537479
Journal Proc Natl Acad Sci U S A
Year 2006
Volume 103
Pages 4022-7
Authors Xu H, Faber C, Uchiki T, Fairman JW, Racca J, Dealwis C
Title Structures of eukaryotic ribonucleotide reductase I provide insights into dNTP regulation.
Related PDB 1zyz 1zzd 2cvs 2cvt 2cvu 2cvv 2cvw 2cvx 2cvy
Related UniProtKB
[7]
Resource
Comments Subunit R1
Medline ID
PubMed ID 16537480
Journal Proc Natl Acad Sci U S A
Year 2006
Volume 103
Pages 4028-33
Authors Xu H, Faber C, Uchiki T, Racca J, Dealwis C
Title Structures of eukaryotic ribonucleotide reductase I define gemcitabine diphosphate binding and subunit assembly.
Related PDB 2eud
Related UniProtKB

Comments
This enzyme belongs to the class I ribonucleotide reductases (RNR). The class I enzyme can be further subdivided into Ia and Ib. This entry is for the subclass Ia, whose subunits are large subunits (R1) and small ones (R2). Moreover, Unlike the other homologous counterpart enzyme, both the subunits have got two different subunits, RNR1 and RNR3 for the large one, and RNR2 and RNR4 for the large one.
The functional form of the small subunits is a RNR2-RNR4 heterodimer, in which RNR2 gives active site for radical generation with cofactor di-iron bound, and RNR4 supports the folding of the RNR2 subunit (see [4]).
Futhermore, this enzyme has different domains, from other counterpart enzymes, at the N-terminus and C-terminus. The tertiary structure of the C-terminal domain, which is an additional domain, has not been determined yet.
The class Ia enzyme has got a allosteric regulation by ATP.
According to the counterpart enzyme from Salmonella typhimurium (M00204 in EzCatDB), this enzyme catalyzes the following reactions:
(A) Electron transfer from thioredoxin (an external donor) to the redox-active Cys883-Cys886 of RNR1 (or Cys864-Cys867 of RNR3) (disulfide) at the C-terminus of the R1 subunit.
(B) Electron transfer from the C-terminus redox-active cysteine pair to the active site redox-active Cys218-Cys443.
(C) Electron transfer from the active site redox-active cysteine pair (Cys218 & Cys443) to the substrate nucleotide.
(D) Radical formation at Tyr183 of the R2 subunit (RNR2):
(E) Radical transfer from Tyr183 to the di-iron site of the R2 subunit (RNR2).
(F) Radical transfer from the di-iron site to the active site Cys428, through Tyr741/Tyr742 of the R1 subunit, generating a thiyl radical at Cys428.
(G) Radical reaction for the substrate nucleotide at the active site Cys428.
#####
Other classes are as follows:
Class I enzymes: M00011 (class Ia), M00204 (class Ib)
Clsss II enzyme (e.g. adenocylcobalamine-dependent rebonucleotide reductase from Lactobacillus leichmannii, E.C 1.17.4.2).
Class III enzyme (E.C. 1.17.4.2): M00203

Created Updated
2004-03-25 2009-02-26