2chv

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2chv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2chv OCA], [http://www.ebi.ac.uk/pdbsum/2chv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2chv RCSB]</span>
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[[Category: nucleotide-binding]]
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Revision as of 23:21, 30 March 2008


PDB ID 2chv

Drag the structure with the mouse to rotate
, resolution 4.00Å
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



REPLICATION FACTOR C ADPNP COMPLEX


Overview

We have investigated the communication between subunits in replication factor C (RFC) from Archaeoglobus fulgidus. Mutation of the proposed arginine finger in the small subunits results in a complex that can still bind ATP but has impaired clamp-loading activity, a process that normally only requires binding of nucleotide. The small subunit alone forms a hexameric ring that is six-fold symmetric in the absence of ATP. However, this symmetry is broken when the nucleotide is bound to the complex. A conformational change associated with nucleotide binding may relate to the opening of PCNA rings by RFC during the loading reaction. The structures also reveal the importance of the N-terminal helix of each subunit at the ATP-binding site. Analysis of mutant protein complexes containing subunits lacking this N-terminal helix reveals key distinct regulatory roles during clamp loading that are different for the large and small subunits in the RFC complex.

About this Structure

2CHV is a Single protein structure of sequence from Archaeoglobus fulgidus. Full crystallographic information is available from OCA.

Reference

Communication between subunits within an archaeal clamp-loader complex., Seybert A, Singleton MR, Cook N, Hall DR, Wigley DB, EMBO J. 2006 May 17;25(10):2209-18. Epub 2006 Apr 20. PMID:16628222

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