1vyi
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The phosphoprotein (P) of rabies virus binds the viral polymerase to the, nucleoprotein (N)-RNA template for transcription and replication. By, limited protease digestion we defined a monomeric C-terminal domain of P, that can bind to N-RNA. The atomic structure of this domain was determined, and previously described mutations that interfere with binding of P to, N-RNA could now be interpreted. There appears to be two features involved, in this activity situated at opposite surfaces of the molecule: a, positively charged patch and a hydrophobic pocket with an exposed, tryptophan side-chain. Other previously published work suggests a, conformational change in P when it binds to N-RNA, which may imply the, repositioning of two helices that would expose a hydrophobic groove for, interaction ... | + | The phosphoprotein (P) of rabies virus binds the viral polymerase to the, nucleoprotein (N)-RNA template for transcription and replication. By, limited protease digestion we defined a monomeric C-terminal domain of P, that can bind to N-RNA. The atomic structure of this domain was determined, and previously described mutations that interfere with binding of P to, N-RNA could now be interpreted. There appears to be two features involved, in this activity situated at opposite surfaces of the molecule: a, positively charged patch and a hydrophobic pocket with an exposed, tryptophan side-chain. Other previously published work suggests a, conformational change in P when it binds to N-RNA, which may imply the, repositioning of two helices that would expose a hydrophobic groove for, interaction with N. This domain of rabies virus P is structurally, unrelated to the N-RNA binding domains of the phosphoproteins of Sendai, and measles virus that are members of the same order of viruses, the, non-segmented negative strand RNA viruses. The implications of this, finding for the evolution of this virus group are discussed. |
==About this Structure== | ==About this Structure== | ||
| - | 1VYI is a | + | 1VYI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rabies_virus Rabies virus] with GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/RNA-directed_RNA_polymerase RNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.48 2.7.7.48] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VYI OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 12:24:29 2007'' |
Revision as of 10:19, 5 November 2007
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STRUCTURE OF THE C-TERMINAL DOMAIN OF THE POLYMERASE COFACTOR OF RABIES VIRUS: INSIGHTS IN FUNCTION AND EVOLUTION.
Overview
The phosphoprotein (P) of rabies virus binds the viral polymerase to the, nucleoprotein (N)-RNA template for transcription and replication. By, limited protease digestion we defined a monomeric C-terminal domain of P, that can bind to N-RNA. The atomic structure of this domain was determined, and previously described mutations that interfere with binding of P to, N-RNA could now be interpreted. There appears to be two features involved, in this activity situated at opposite surfaces of the molecule: a, positively charged patch and a hydrophobic pocket with an exposed, tryptophan side-chain. Other previously published work suggests a, conformational change in P when it binds to N-RNA, which may imply the, repositioning of two helices that would expose a hydrophobic groove for, interaction with N. This domain of rabies virus P is structurally, unrelated to the N-RNA binding domains of the phosphoproteins of Sendai, and measles virus that are members of the same order of viruses, the, non-segmented negative strand RNA viruses. The implications of this, finding for the evolution of this virus group are discussed.
About this Structure
1VYI is a Single protein structure of sequence from Rabies virus with GOL as ligand. Active as RNA-directed RNA polymerase, with EC number 2.7.7.48 Structure known Active Site: AC1. Full crystallographic information is available from OCA.
Reference
Structure and function of the C-terminal domain of the polymerase cofactor of rabies virus., Mavrakis M, McCarthy AA, Roche S, Blondel D, Ruigrok RW, J Mol Biol. 2004 Oct 29;343(4):819-31. PMID:15476803
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