1gx6

File:1gx6.gif

spinqualitylabelsall models 1gx6, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

HEPATITIS C VIRUS RNA POLYMERASE IN COMPLEX WITH UTP AND MANGANESE

OverviewOverview

We report here the results of a systematic high-resolution X-ray, crystallographic analysis of complexes of the hepatitis C virus (HCV) RNA, polymerase with ribonucleoside triphosphates (rNTPs) and divalent metal, ions. An unexpected observation revealed by this study is the existence of, a specific rGTP binding site in a shallow pocket at the molecular surface, of the enzyme, 30 A away from the catalytic site. This previously, unidentified rGTP pocket, which lies at the interface between fingers and, thumb, may be an allosteric regulatory site and could play a role in, allowing alternative interactions between the two domains during a, possible conformational change of the enzyme required for efficient, initiation. The electron density map at 1.7-A resolution clearly shows the, mode of ... [(full description)]

About this StructureAbout this Structure

1GX6 is a [Single protein] structure of sequence from [Hepatitis c virus genotype 1b (isolate bk)] with MN and UTP as [ligands]. Active as [RNA-directed RNA polymerase], with EC number [2.7.7.48]. Structure known Active Site: UT1. Full crystallographic information is available from [OCA].

ReferenceReference

Structural analysis of the hepatitis C virus RNA polymerase in complex with ribonucleotides., Bressanelli S, Tomei L, Rey FA, De Francesco R, J Virol. 2002 Apr;76(7):3482-92. PMID:11884572

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