2chg: Difference between revisions
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==Overview== | ==Overview== | ||
We have investigated the communication between subunits in replication | 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== | ==About this Structure== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Cook, N.]] | [[Category: Cook, N.]] | ||
[[Category: Hall, D | [[Category: Hall, D R.]] | ||
[[Category: Seybert, A.]] | [[Category: Seybert, A.]] | ||
[[Category: Singleton, M | [[Category: Singleton, M R.]] | ||
[[Category: Wigley, D | [[Category: Wigley, D B.]] | ||
[[Category: ANP]] | [[Category: ANP]] | ||
[[Category: MG]] | [[Category: MG]] | ||
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[[Category: nucleotide-binding]] | [[Category: nucleotide-binding]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:48:39 2008'' | ||
Revision as of 14:48, 21 February 2008
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REPLICATION FACTOR C DOMAINS 1 AND 2
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
2CHG is a Single protein structure of sequence from Archaeoglobus fulgidus with MG and ANP as ligands. Known structural/functional Site: AC1. 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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