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2chg

From Proteopedia

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{{STRUCTURE_2chg| PDB=2chg | SCENE= }}
{{STRUCTURE_2chg| PDB=2chg | SCENE= }}
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'''REPLICATION FACTOR C DOMAINS 1 AND 2'''
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===REPLICATION FACTOR C DOMAINS 1 AND 2===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_16628222}}
==About this Structure==
==About this Structure==
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[[Category: Dna-binding protein]]
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[[Category: Nucleotide-binding]]
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Revision as of 10:15, 29 July 2008

Image:2chg.png

Template:STRUCTURE 2chg

REPLICATION FACTOR C DOMAINS 1 AND 2

Template:ABSTRACT PUBMED 16628222

About this Structure

2CHG 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

Page seeded by OCA on Tue Jul 29 13:15:08 2008

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