1hi0: Difference between revisions

Revision as of 08:12, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1hi0.png

Template:STRUCTURE 1hi0

RNA DEPENDENT RNA POLYMERASE FROM DSRNA BACTERIOPHAGE PHI6 PLUS INITIATION COMPLEXRNA DEPENDENT RNA POLYMERASE FROM DSRNA BACTERIOPHAGE PHI6 PLUS INITIATION COMPLEX

Template:ABSTRACT PUBMED 11242087

About this StructureAbout this Structure

1HI0 is a Single protein structure of sequence from Pseudomonas phage phi6. Full crystallographic information is available from OCA.

ReferenceReference

A mechanism for initiating RNA-dependent RNA polymerization., Butcher SJ, Grimes JM, Makeyev EV, Bamford DH, Stuart DI, Nature. 2001 Mar 8;410(6825):235-40. PMID:11242087

Page seeded by OCA on Tue Jul 1 08:12:36 2008

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 {{STRUCTURE_1hi0|  PDB=1hi0  |  SCENE=  }}
-'''RNA DEPENDENT RNA POLYMERASE FROM DSRNA BACTERIOPHAGE PHI6 PLUS INITIATION COMPLEX'''
+===RNA DEPENDENT RNA POLYMERASE FROM DSRNA BACTERIOPHAGE PHI6 PLUS INITIATION COMPLEX===
-==Overview==
+<!--
-In most RNA viruses, genome replication and transcription are catalysed by a viral RNA-dependent RNA polymerase. Double-stranded RNA viruses perform these operations in a capsid (the polymerase complex), using an enzyme that can read both single- and double-stranded RNA. Structures have been solved for such viral capsids, but they do not resolve the polymerase subunits in any detail. Here we show that the 2 A resolution X-ray structure of the active polymerase subunit from the double-stranded RNA bacteriophage straight phi6 is highly similar to that of the polymerase of hepatitis C virus, providing an evolutionary link between double-stranded RNA viruses and flaviviruses. By crystal soaking and co-crystallization, we determined a number of other structures, including complexes with oligonucleotide and/or nucleoside triphosphates (NTPs), that suggest a mechanism by which the incoming double-stranded RNA is opened up to feed the template through to the active site, while the substrates enter by another route. The template strand initially overshoots, locking into a specificity pocket, and then, in the presence of cognate NTPs, reverses to form the initiation complex; this process engages two NTPs, one of which acts with the carboxy-terminal domain of the protein to prime the reaction. Our results provide a working model for the initiation of replication and transcription.
+The line below this paragraph, {{ABSTRACT_PUBMED_11242087}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11242087 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11242087}}
 ==About this Structure==
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 [[Category: Rna polymerase]]
 [[Category: Viral polymerase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 18:51:55 2008''
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