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CATH domain | Related DB codes (homologues) |
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3.40.50.150 : Rossmann fold | S00637,S00639,S00262,S00261,S00291,D00075,D00076,D00079,D00080,D00082,D00083,D00823 |
Enzyme Name | UniProtKB | KEGG |
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| P07617 |
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Protein name | Cap-specific mRNA (nucleoside-2''-O-)-methyltransferase | mRNA (nucleoside-2'-O-)-methyltransferasemessenger ribonucleate nucleoside 2'-methyltransferasemessenger RNA (nucleoside-2'-)-methyltransferase |
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Synonyms | EC 2.1.1.57Poly(A) polymerase regulatory subunitPoly(A) polymerase small subunitPAP-SVP39 |
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RefSeq | YP_232977.1 (Protein) NC_006998.1 (DNA/RNA sequence)
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Pfam | PF01358 (PARP_regulatory) [Graphical view]
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UniProtKB:Accession Number | P07617 |
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Entry name | PAP2_VACCV |
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Activity | S-adenosyl-L-methionine + m(7)G(5'')pppR-RNA = S-adenosyl-L-homocysteine + m(7)G(5'')pppRm-RNA. |
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Subunit | Methyltransferase activity: Monomer, poly(A) polymerase activity: Heterodimer of VP55 (catalytic) and VP39 (regulatory). |
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Subcellular location |
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Cofactor |
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References for Catalytic Mechanism | References | Sections | No. of steps in catalysis |
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[8] | p.446 |
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references | [1] |
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PubMed ID | 1670500 |
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Journal | Cell |
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Year | 1991 |
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Volume | 66 |
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Pages | 1269-78 |
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Authors | Gershon PD, Ahn BY, Garfield M, Moss B |
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Title | Poly(A) polymerase and a dissociable polyadenylation stimulatory factor encoded by vaccinia virus. |
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Related UniProtKB | P07617 |
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[2] |
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PubMed ID | 1313572 |
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Journal | Proc Natl Acad Sci U S A |
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Year | 1992 |
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Volume | 89 |
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Pages | 2897-901 |
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Authors | Schnierle BS, Gershon PD, Moss B |
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Title | Cap-specific mRNA (nucleoside-O2'-)-methyltransferase and poly(A) polymerase stimulatory activities of vaccinia virus are mediated by a single protein. |
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Related UniProtKB | P07617 |
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[3] |
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PubMed ID | 8846300 |
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Journal | RNA |
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Year | 1996 |
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Volume | 2 |
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Pages | 88-101 |
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Authors | Shi X, Yao P, Jose T, Gershon P |
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Title | Methyltransferase-specific domains within VP-39, a bifunctional protein that participates in the modification of both mRNA ends. |
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[4] |
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PubMed ID | 8612277 |
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Journal | Cell |
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Year | 1996 |
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Volume | 85 |
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Pages | 247-56 |
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Authors | Hodel AE, Gershon PD, Shi X, Quiocho FA |
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Title | The 1.85 A structure of vaccinia protein VP39: a bifunctional enzyme that participates in the modification of both mRNA ends. |
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Related PDB | 1vpt |
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Related UniProtKB | P07617 |
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[5] |
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PubMed ID | 9118948 |
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Journal | EMBO J |
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Year | 1997 |
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Volume | 16 |
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Pages | 1103-13 |
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Authors | Deng L, Gershon PD |
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Title | Interplay of two uridylate-specific RNA binding sites in the translocation of poly(A) polymerase from vaccinia virus. |
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[6] |
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PubMed ID | 9145102 |
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Journal | Nat Struct Biol |
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Year | 1997 |
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Volume | 4 |
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Pages | 350-4 |
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Authors | Hodel AE, Gershon PD, Shi X, Wang SM, Quiocho FA |
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Title | Specific protein recognition of an mRNA cap through its alkylated base. |
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Related PDB | 1p39,1v39,1vp3,1vp9,2vp3 |
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[7] |
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PubMed ID | 9287339 |
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Journal | J Biol Chem |
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Year | 1997 |
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Volume | 272 |
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Pages | 23292-302 |
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Authors | Shi X, Bernhardt TG, Wang SM, Gershon PD |
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Title | The surface region of the bifunctional vaccinia RNA modifying protein VP39 that interfaces with Poly(A) polymerase is remote from the RNA binding cleft used for its mRNA 5' cap methylation function. |
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[8] |
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PubMed ID | 9660928 |
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Journal | Mol Cell |
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Year | 1998 |
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Volume | 1 |
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Pages | 443-7 |
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Authors | Hodel AE, Gershon PD, Quiocho FA |
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Title | Structural basis for sequence-nonspecific recognition of 5'-capped mRNA by a cap-modifying enzyme. |
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Related PDB | 1av6 |
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Related UniProtKB | P07617 |
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[9] |
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PubMed ID | 9622508 |
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Journal | Biochemistry |
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Year | 1998 |
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Volume | 37 |
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Pages | 8564-74 |
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Authors | Lockless SW, Cheng HT, Hodel AE, Quiocho FA, Gershon PD |
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Title | Recognition of capped RNA substrates by VP39, the vaccinia virus-encoded mRNA cap-specific 2'-O-methyltransferase. |
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[10] |
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PubMed ID | 9657944 |
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Journal | Virology |
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Year | 1998 |
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Volume | 246 |
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Pages | 253-65 |
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Authors | Gershon PD, Shi X, Hodel AE |
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Title | Evidence that the RNA methylation and poly(A) polymerase stimulatory activities of vaccinia virus protein VP39 do not impinge upon one another. |
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[11] |
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PubMed ID | 9917386 |
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Journal | J Mol Biol |
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Year | 1999 |
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Volume | 285 |
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Pages | 1417-27 |
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Authors | Deng L, Johnson L, Neveu JM, Hardin S, Wang SM, Lane WS, Gershon PD |
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Title | A polyadenylylation-specific RNA-contact site on the surface of the bifunctional vaccinia virus RNA modifying protein VP39 that is distinct from the mRNA 5' end-binding "cleft". |
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[12] |
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PubMed ID | 10377383 |
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Journal | Proc Natl Acad Sci U S A |
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Year | 1999 |
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Volume | 96 |
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Pages | 7149-54 |
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Authors | Hu G, Gershon PD, Hodel AE, Quiocho FA |
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Title | mRNA cap recognition: dominant role of enhanced stacking interactions between methylated bases and protein aromatic side chains. |
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Related PDB | 1b42,1bky,1eam,1eqa,3mag,3mct,4dcg |
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[13] |
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Comments | Review |
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PubMed ID | 10766517 |
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Journal | Curr Opin Struct Biol |
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Year | 2000 |
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Volume | 10 |
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Pages | 75-7 |
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Authors | Rhodes D, Burley SK |
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Title | Protein-nucleic acid interactions. |
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[14] |
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Comments | Review |
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PubMed ID | 10679461 |
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Journal | Curr Opin Struct Biol |
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Year | 2000 |
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Volume | 10 |
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Pages | 78-86 |
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Authors | Quiocho FA, Hu G, Gershon PD |
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Title | Structural basis of mRNA cap recognition by proteins. |
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[15] |
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PubMed ID | 11076512 |
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Journal | Biochemistry |
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Year | 2000 |
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Volume | 39 |
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Pages | 13730-6 |
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Authors | Hsu PC, Hodel MR, Thomas JW, Taylor LJ, Hagedorn CH, Hodel AE |
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Title | Structural requirements for the specific recognition of an m7G mRNA cap. |
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[16] |
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PubMed ID | 12056899 |
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Journal | Biochemistry |
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Year | 2002 |
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Volume | 41 |
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Pages | 7677-87 |
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Authors | Hu G, Oguro A, Li C, Gershon PD, Quiocho FA |
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Title | The "cap-binding slot" of an mRNA cap-binding protein: quantitative effects of aromatic side chain choice in the double-stacking sandwich with cap. |
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Related PDB | 1jsz,1jte,1jtf |
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comments | This enzyme is a bifunctional protein, which methylates the ribose 2' OH group of the first transcribed nucleotide, and also act as a regulatory subunit of poly(A) polymerase, VP55, which creates the 3' poly(A) tail of mRNA's. This protein binds to poly(A), as a regulatory subunit. According to the literature [8], the active site of this enzyme is similar to that of COMT (S00291 in EzCatDB), although it does not utilize a cofactor magnesium ion, unlike COMT. According to the literature [8], the reaction proceeds as follows: (1) The positively charged sidechains of Lys41 and Lys175 act as modulator, which activate the acceptor, the oxygen atom of the 2' OH group, by lowering the pKa of the acceptor group, together with the positively charged sulfur atom of another substrate, SAM. (2) The activated acceptor group makes a nucleophilic attack on the transferred group, the methyl group of SAM. (Probably, the reaction proceeds through an SN2-like mechanism, leading to the inversion of configuration of the methyl group, as in COMT.)
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created | updated |
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2002-08-30 | 2009-02-26 |
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