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1vyi
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The phosphoprotein (P) of rabies virus binds the viral polymerase to the | + | 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== | ||
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[[Category: Blondel, D.]] | [[Category: Blondel, D.]] | ||
[[Category: Mavrakis, M.]] | [[Category: Mavrakis, M.]] | ||
| - | [[Category: Mccarthy, A | + | [[Category: Mccarthy, A A.]] |
[[Category: Roche, S.]] | [[Category: Roche, S.]] | ||
| - | [[Category: Ruigrok, R | + | [[Category: Ruigrok, R W.H.]] |
[[Category: GOL]] | [[Category: GOL]] | ||
[[Category: phosphorylation]] | [[Category: phosphorylation]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:38:40 2008'' |
Revision as of 13:38, 21 February 2008
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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 as ligand. Active as RNA-directed RNA polymerase, with EC number 2.7.7.48 Known structural/functional Site: . 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
Page seeded by OCA on Thu Feb 21 15:38:40 2008
