2e9z: Difference between revisions

Revision as of 09:37, 28 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:2e9z.png

Template:STRUCTURE 2e9z

Foot-and-mouth disease virus RNA-polymerase in complex with a template- primer RNA, ATP and UTPFoot-and-mouth disease virus RNA-polymerase in complex with a template- primer RNA, ATP and UTP

Template:ABSTRACT PUBMED 17517631

About this StructureAbout this Structure

2E9Z is a Single protein structure of sequence from Foot-and-mouth disease virus. Full crystallographic information is available from OCA.

ReferenceReference

Sequential structures provide insights into the fidelity of RNA replication., Ferrer-Orta C, Arias A, Perez-Luque R, Escarmis C, Domingo E, Verdaguer N, Proc Natl Acad Sci U S A. 2007 May 29;104(22):9463-8. Epub 2007 May 21. PMID:17517631

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Foot-and-mouth disease virus RNA-polymerase in complex with a template- primer RNA, ATP and UTP'''
+===Foot-and-mouth disease virus RNA-polymerase in complex with a template- primer RNA, ATP and UTP===
-==Overview==
+<!--
-RNA virus replication is an error-prone event caused by the low fidelity of viral RNA-dependent RNA polymerases. Replication fidelity can be decreased further by the use of mutagenic ribonucleoside analogs to a point where viral genetic information can no longer be maintained. For foot-and-mouth disease virus, the antiviral analogs ribavirin and 5-fluorouracil have been shown to be mutagenic, contributing to virus extinction through lethal mutagenesis. Here, we report the x-ray structure of four elongation complexes of foot-and-mouth disease virus polymerase 3D obtained in presence of natural substrates, ATP and UTP, or mutagenic nucleotides, ribavirin triphosphate and 5-fluorouridine triphosphate with different RNAs as template-primer molecules. The ability of these complexes to synthesize RNA in crystals allowed us to capture different successive replication events and to define the critical amino acids involved in (i) the recognition and positioning of the incoming nucleotide or analog; (ii) the positioning of the acceptor base of the template strand; and (iii) the positioning of the 3'-OH group of the primer nucleotide during RNA replication. The structures identify key interactions involved in viral RNA replication and provide insights into the molecular basis of the low fidelity of viral RNA polymerases.
+The line below this paragraph, {{ABSTRACT_PUBMED_17517631}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17517631 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_17517631}}
 ==About this Structure==
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 [[Category: Polymerase]]
 [[Category: Rna-dependent rna polymerase]]
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