DB code: D00510
RLCP classification | 1.13.30100.19 : Hydrolysis | |
---|---|---|
CATH domain | 2.10.109.10 : Umud Fragment, subunit A | Catalytic domain |
1.10.10.10 : Arc Repressor Mutant, subunit A | ||
E.C. | 3.4.21.88 | |
CSA | 1jhf | |
M-CSA | 1jhf | |
MACiE |
CATH domain | Related DB codes (homologues) |
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1.10.10.10 : Arc Repressor Mutant, subunit A | D00452 D00077 D00517 T00055 T00113 |
Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | RefSeq | MEROPS | Pfam |
---|---|---|---|---|---|
P0A7C2 |
LexA repressor
|
EC
3.4.21.88
|
NP_418467.1
(Protein)
NC_000913.2 (DNA/RNA sequence) YP_492186.1 (Protein) NC_007779.1 (DNA/RNA sequence) |
S24.001
(Serine)
|
PF01726
(LexA_DNA_bind)
PF00717 (Peptidase_S24) [Graphical View] |
KEGG enzyme name |
---|
repressor LexA
LexA repressor |
UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
---|---|---|---|---|---|
P0A7C2 | LEXA_ECOLI | Hydrolysis of Ala-|-Gly bond in repressor lexA. | Homodimer. |
KEGG Pathways | Map code | Pathways | E.C. |
---|
Compound table | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Substrates | Products | Intermediates | ||||||||||
KEGG-id | C99999 | C00001 | C00017 | C00012 | I00087 | I00085 | I00086 | |||||
E.C. | ||||||||||||
Compound | Repressor LexA | H2O | Protein | Peptide | Peptidyl-tetrahedral intermediate | Acyl-enzyme | Tetrahedral intermediate | |||||
Type | peptide/protein | H2O | peptide/protein | |||||||||
ChEBI |
15377 |
|||||||||||
PubChem |
962 22247451 |
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1jhcA |
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Unbound | Unbound | Unbound | ||||
1jheA |
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Bound:ALA_84-GLY_85 (chain A) | Unbound | Unbound | ||||
1jheB |
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Bound:ALA_84-GLY_85 (chain B) | Unbound | Unbound | ||||
1jhfA01 |
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Unbound | Unbound | Unbound | ||||
1jhfB |
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Unbound | Unbound | Unbound | ||||
1jhhA01 |
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Unbound | Unbound | Unbound | ||||
1jhhB |
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Bound:ALA_84-GLY_85 (chain B) | Unbound | Unbound | ||||
1jhfA02 |
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Unbound | Unbound | Unbound | ||||
1jhhA02 |
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Unbound | Unbound | Unbound | ||||
1leaA |
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Unbound | Unbound | Unbound | ||||
1lebA |
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Unbound | Unbound | Unbound |
Reference for Active-site residues | ||
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resource | references | E.C. |
literature [4], [8], [13], [28] |
Active-site residues | ||||||||||
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PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
1jhcA |
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;LYS 156 | MET 118; | mutant S119A | ||
1jheA |
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SER 119; | MET 118;SER 119 | mutant L89P, Q92W, E152A, K156A | ||
1jheB |
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SER 119; | MET 118;SER 119 | mutant L89P, Q92W, E152A, K156A | ||
1jhfA01 |
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SER 119;LYS 156 | MET 118;SER 119 | mutant G85D | ||
1jhfB |
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SER 119;LYS 156 | MET 118;SER 119 | |||
1jhhA01 |
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;LYS 156 | MET 118; | mutant S119A | ||
1jhhB |
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;LYS 156 | MET 118; | mutant S119A | ||
1jhfA02 |
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1jhhA02 |
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1leaA |
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1lebA |
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References for Catalytic Mechanism | ||
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References | Sections | No. of steps in catalysis |
[4]
|
Fig.4, p.3990-3991 | |
[8]
|
Fig.1, p.12834-12835 | |
[10]
|
Fig.2, p.416-417 | |
[13]
|
p.921-922 | |
[28]
|
p.588-589 |
References | |
---|---|
[1] | |
Resource | |
Comments | FUNCTION. |
Medline ID | 82037807 |
PubMed ID | 7027256 |
Journal | Proc Natl Acad Sci U S A |
Year | 1981 |
Volume | 78 |
Pages | 4204-8 |
Authors | Brent R, Ptashne M |
Title | Mechanism of action of the lexA gene product. |
Related PDB | |
Related UniProtKB | P0A7C2 |
[2] | |
Resource | |
Comments | FUNCTION. |
Medline ID | 82037806 |
PubMed ID | 7027255 |
Journal | Proc Natl Acad Sci U S A |
Year | 1981 |
Volume | 78 |
Pages | 4199-203 |
Authors | Little JW, Mount DW, Yanisch-Perron CR |
Title | Purified lexA protein is a repressor of the recA and lexA genes. |
Related PDB | |
Related UniProtKB | P0A7C2 |
[3] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 3709524 |
Journal | EMBO J |
Year | 1986 |
Volume | 5 |
Pages | 793-8 |
Authors | Hurstel S, Granger-Schnarr M, Daune M, Schnarr M |
Title | In vitro binding of LexA repressor to DNA: evidence for the involvement of the amino-terminal domain. |
Related PDB | |
Related UniProtKB | |
[4] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 3108885 |
Journal | Proc Natl Acad Sci U S A |
Year | 1987 |
Volume | 84 |
Pages | 3987-91 |
Authors | Slilaty SN, Little JW |
Title | Lysine-156 and serine-119 are required for LexA repressor cleavage: a possible mechanism. |
Related PDB | |
Related UniProtKB | |
[5] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 2834329 |
Journal | J Bacteriol |
Year | 1988 |
Volume | 170 |
Pages | 2163-73 |
Authors | Lin LL, Little JW |
Title | Isolation and characterization of noncleavable (Ind-) mutants of the LexA repressor of Escherichia coli K-12. |
Related PDB | |
Related UniProtKB | |
[6] | |
Resource | |
Comments | STRUCTURE BY NMR. |
Medline ID | 89386639 |
PubMed ID | 2780544 |
Journal | Proc Natl Acad Sci U S A |
Year | 1989 |
Volume | 86 |
Pages | 6863-7 |
Authors | Lamerichs RM, Padilla A, Boelens R, Kaptein R, Ottleben G, Ruterjans H, Granger-Schnarr M, Oertel P, Schnarr M |
Title | The amino-terminal domain of LexA repressor is alpha-helical but differs from canonical helix-turn-helix proteins: a two-dimensional 1H NMR study. |
Related PDB | |
Related UniProtKB | P0A7C2 |
[7] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 2184894 |
Journal | Biochemistry |
Year | 1990 |
Volume | 29 |
Pages | 1961-70 |
Authors | Hurstel S, Granger-Schnarr M, Schnarr M |
Title |
The LexA repressor and its isolated amino-terminal domain interact cooperatively with poly[d(A-T)], |
Related PDB | |
Related UniProtKB | |
[8] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 2198279 |
Journal | J Biol Chem |
Year | 1990 |
Volume | 265 |
Pages | 12828-35 |
Authors | Roland KL, Little JW |
Title |
Reaction of LexA repressor with diisopropyl fluorophosphate. |
Related PDB | |
Related UniProtKB | |
[9] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 2259342 |
Journal | Mol Gen Genet |
Year | 1990 |
Volume | 223 |
Pages | 40-8 |
Authors | Oertel-Buchheit P, Lamerichs RM, Schnarr M, Granger-Schnarr M |
Title | Genetic analysis of the LexA repressor: isolation and characterization of LexA(Def) mutant proteins. |
Related PDB | |
Related UniProtKB | |
[10] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 1911941 |
Journal | Biochimie |
Year | 1991 |
Volume | 73 |
Pages | 411-21 |
Authors | Little JW |
Title | Mechanism of specific LexA cleavage: autodigestion and the role of RecA coprotease. |
Related PDB | |
Related UniProtKB | |
[11] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 1911942 |
Journal | Biochimie |
Year | 1991 |
Volume | 73 |
Pages | 423-31 |
Authors | Schnarr M, Oertel-Buchheit P, Kazmaier M, Granger-Schnarr M |
Title | DNA binding properties of the LexA repressor. |
Related PDB | |
Related UniProtKB | |
[12] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 1815638 |
Journal | J Biomol Struct Dyn |
Year | 1991 |
Volume | 9 |
Pages | 447-61 |
Authors | Ottleben G, Messori L, Ruterjans H, Kaptein R, Granger-Schnarr M, Schnarr M |
Title | 1H-NMR investigation of the interaction of the amino terminal domain of the LexA repressor with a synthetic half-operator. |
Related PDB | |
Related UniProtKB | |
[13] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 1667880 |
Journal | Protein Eng |
Year | 1991 |
Volume | 4 |
Pages | 919-22 |
Authors | Slilaty SN, Vu HK |
Title | The role of electrostatic interactions in the mechanism of peptide bond hydrolysis by a Ser-Lys catalytic dyad. |
Related PDB | |
Related UniProtKB | |
[14] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 1602473 |
Journal | J Mol Biol |
Year | 1992 |
Volume | 225 |
Pages | 609-20 |
Authors | Oertel-Buchheit P, Porte D, Schnarr M, Granger-Schnarr M |
Title | Isolation and characterization of LexA mutant repressors with enhanced DNA binding affinity. |
Related PDB | |
Related UniProtKB | |
[15] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 1453451 |
Journal | J Mol Biol |
Year | 1992 |
Volume | 228 |
Pages | 395-408 |
Authors | Roland KL, Smith MH, Rupley JA, Little JW |
Title | In vitro analysis of mutant LexA proteins with an increased rate of specific cleavage. |
Related PDB | |
Related UniProtKB | |
[16] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 1620111 |
Journal | Mol Cell Biol |
Year | 1992 |
Volume | 12 |
Pages | 3006-14 |
Authors | Golemis EA, Brent R |
Title | Fused protein domains inhibit DNA binding by LexA. |
Related PDB | |
Related UniProtKB | |
[17] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 8513500 |
Journal | Cell |
Year | 1993 |
Volume | 73 |
Pages | 1165-73 |
Authors | Kim B, Little JW |
Title | LexA and lambda Cl repressors as enzymes: specific cleavage in an intermolecular reaction. |
Related PDB | |
Related UniProtKB | |
[18] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 8349538 |
Journal | J Bacteriol |
Year | 1993 |
Volume | 175 |
Pages | 4943-50 |
Authors | Little JW |
Title | LexA cleavage and other self-processing reactions. |
Related PDB | |
Related UniProtKB | |
[19] | |
Resource | |
Comments | STRUCTURE BY NMR. |
Medline ID | 94357165 |
PubMed ID | 8076591 |
Journal | EMBO J |
Year | 1994 |
Volume | 13 |
Pages | 3936-44 |
Authors | Fogh RH, Ottleben G, Ruterjans H, Schnarr M, Boelens R, Kaptein R |
Title | Solution structure of the LexA repressor DNA binding domain determined by 1H NMR spectroscopy. |
Related PDB | 1lea 1leb |
Related UniProtKB | P0A7C2 |
[20] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 7716155 |
Journal | Protein Eng |
Year | 1994 |
Volume | 7 |
Pages | 1449-53 |
Authors | Holm L, Sander C, Ruterjans H, Schnarr M, Fogh R, Boelens R, Kaptein R |
Title | LexA repressor and iron uptake regulator from Escherichia coli: new members of the CAP-like DNA binding domain superfamily. |
Related PDB | |
Related UniProtKB | |
[21] | |
Resource | |
Comments | 3D-STRUCTURE MODELING. |
Medline ID | 95303877 |
PubMed ID | 7784426 |
Journal | Proteins |
Year | 1995 |
Volume | 21 |
Pages | 226-36 |
Authors | Knegtel RM, Fogh RH, Ottleben G, Ruterjans H, Dumoulin P, Schnarr M, Boelens R, Kaptein R |
Title | A model for the LexA repressor DNA complex. |
Related PDB | |
Related UniProtKB | P0A7C2 |
[22] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 8605176 |
Journal | Biochemistry |
Year | 1996 |
Volume | 35 |
Pages | 4279-86 |
Authors | Dumoulin P, Ebright RH, Knegtel R, Kaptein R, Granger-Schnarr M, Schnarr M |
Title | Structure of the LexA repressor-DNA complex probed by affinity cleavage and affinity photo-cross-linking. |
Related PDB | |
Related UniProtKB | |
[23] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 8876169 |
Journal | Proc Natl Acad Sci U S A |
Year | 1996 |
Volume | 93 |
Pages | 11528-33 |
Authors | Shepley DP, Little JW |
Title | Mutant LexA proteins with specific defects in autodigestion. |
Related PDB | |
Related UniProtKB | |
[24] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 9512712 |
Journal | J Mol Biol |
Year | 1998 |
Volume | 276 |
Pages | 405-15 |
Authors | Konola JT, Guzzo A, Gow JB, Walker GC, Knight KL |
Title | Differential cleavage of LexA and UmuD mediated by recA Pro67 mutants: implications for common LexA and UmuD binding sites on RecA. |
Related PDB | |
Related UniProtKB | |
[25] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 9521130 |
Journal | Protein Sci |
Year | 1998 |
Volume | 7 |
Pages | 512-5 |
Authors | Oertel-Buchheit P, Reinbolt J, John M, Granger-Schnarr M, Schnarr M |
Title | A LexA mutant repressor with a relaxed inter-domain linker. |
Related PDB | |
Related UniProtKB | |
[26] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 10692372 |
Journal | J Bacteriol |
Year | 2000 |
Volume | 182 |
Pages | 1659-70 |
Authors | Mustard JA, Little JW |
Title |
Analysis of Escherichia coli RecA interactions with LexA, |
Related PDB | |
Related UniProtKB | |
[27] | |
Resource | |
Comments | Model |
Medline ID | |
PubMed ID | 11089640 |
Journal | J Biomol Struct Dyn |
Year | 2000 |
Volume | 18 |
Pages | 181-97 |
Authors | Chattopadhyaya R, Ghosh K, Namboodiri VM |
Title | Model of a LexA repressor dimer bound to recA operator. |
Related PDB | 1qaa |
Related UniProtKB | |
[28] | |
Resource | |
Comments | X-RAY DIFFRACTION |
Medline ID | |
PubMed ID | 11551506 |
Journal | Cell |
Year | 2001 |
Volume | 106 |
Pages | 585-94 |
Authors | Luo Y, Pfuetzner RA, Mosimann S, Paetzel M, Frey EA, Cherney M, Kim B, Little JW, Strynadka NC |
Title | Crystal structure of LexA: a conformational switch for regulation of self-cleavage. |
Related PDB | 1jhc 1jhe 1jhf 1jhh |
Related UniProtKB | |
[29] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 11583611 |
Journal | Mol Cell |
Year | 2001 |
Volume | 8 |
Pages | 486-7 |
Authors | Walker GC |
Title | To cleave or not to cleave? Insights from the LexA crystal structure. |
Related PDB | |
Related UniProtKB | |
[30] | |
Resource | |
Comments | Model |
Medline ID | |
PubMed ID | 14769061 |
Journal | J Biomol Struct Dyn |
Year | 2004 |
Volume | 21 |
Pages | 681-9 |
Authors | Chattopadhyaya R, Pal A |
Title | Improved model of a LexA repressor dimer bound to recA operator. |
Related PDB | 1mvd |
Related UniProtKB | |
[31] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 15929009 |
Journal | J Biomol NMR |
Year | 2005 |
Volume | 31 |
Pages | 371-2 |
Authors | Okon M, Pfuetzner RA, Vuckovic M, Little JW, Strynadka NC, McIntosh LP |
Title | Backbone chemical shift assignments of the LexA catalytic domain in its active conformation. |
Related PDB | |
Related UniProtKB |
Comments |
---|
This enzyme belongs to the peptidase family-S24.
This enzyme performs auto-catalysis (or auto-hydrolysis). According to the literature [4], (1) Lys156 acts as a general base to deprotonate the nucleophile, (2) Ser119 makes a nucleophilic attack on the carbonyl carbon atom of the target peptide bond (Ala84-Gly85), (3) The negative charge of the tetrahedral transition state is stabilized by the oxyanion hole, (4) Lys156 acts as a general acid to protonate the leaving amino group, (5) Lys156 probably acts as a general base to deprotonate and activate a water molecule. (6) The activated water makes a nucleophilic attack on the carbonyl carbon of the intermediate. (7) Lys156 acts as a general acid to protonate Ser119, |
Created | Updated |
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2003-08-22 | 2011-02-21 |