2chq

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==Overview==
==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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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.]]
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[[Category: Hall, D.R.]]
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[[Category: Hall, D R.]]
[[Category: Seybert, A.]]
[[Category: Seybert, A.]]
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[[Category: Singleton, M.R.]]
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[[Category: Singleton, M R.]]
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[[Category: Wigley, D.B.]]
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[[Category: Wigley, D B.]]
[[Category: ANP]]
[[Category: ANP]]
[[Category: aaa+ atpase]]
[[Category: aaa+ atpase]]
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[[Category: nucleotide-binding]]
[[Category: nucleotide-binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:35:26 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:48:44 2008''

Revision as of 14:48, 21 February 2008


2chq, resolution 3.50Å

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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

2CHQ is a Single protein structure of sequence from Archaeoglobus fulgidus with as ligand. Known structural/functional Site: . 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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