This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1vyi
From Proteopedia
| Line 12: | Line 12: | ||
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15476803 15476803] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15476803 15476803] | ||
| + | [[Category: RNA-directed RNA polymerase]] | ||
[[Category: Rabies virus]] | [[Category: Rabies virus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 28: | Line 29: | ||
[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:01:47 2007'' |
Revision as of 07:57, 30 October 2007
|
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 ... [(full description)]
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
Page seeded by OCA on Tue Oct 30 10:01:47 2007
