1c2p
From Proteopedia
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| , resolution 1.90Å | |||||||
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| Activity: | RNA-directed RNA polymerase, with EC number 2.7.7.48 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HEPATITIS C VIRUS NS5B RNA-DEPENDENT RNA POLYMERASE
Overview
Various classes of nucleotidyl polymerases with different transcriptional roles contain a conserved core structure. Less is known, however, about the distinguishing features of these enzymes, particularly those of the RNA-dependent RNA polymerase class. The 1. 9 A resolution crystal structure of hepatitis C virus (HCV) nonstructural protein 5B (NS5B) presented here provides the first complete and detailed view of an RNA-dependent RNA polymerase. While canonical polymerase features exist in the structure, NS5B adopts a unique shape due to extensive interactions between the fingers and thumb polymerase subdomains that serve to encircle the enzyme active site. Several insertions in the fingers subdomain account for intersubdomain linkages that include two extended loops and a pair of antiparallel alpha-helices. The HCV NS5B apoenzyme structure reported here can accommodate a template:primer duplex without global conformational changes, supporting the hypothesis that this structure is essentially preserved during the reaction pathway. This NS5B template:primer model also allows identification of a new structural motif involved in stabilizing the nascent base pair.
About this Structure
1C2P is a Single protein structure of sequence from Hepatitis c virus. Full crystallographic information is available from OCA.
Reference
Crystal structure of the RNA-dependent RNA polymerase from hepatitis C virus reveals a fully encircled active site., Lesburg CA, Cable MB, Ferrari E, Hong Z, Mannarino AF, Weber PC, Nat Struct Biol. 1999 Oct;6(10):937-43. PMID:10504728
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