2chq
From Proteopedia
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|PDB= 2chq |SIZE=350|CAPTION= <scene name='initialview01'>2chq</scene>, resolution 3.50Å | |PDB= 2chq |SIZE=350|CAPTION= <scene name='initialview01'>2chq</scene>, resolution 3.50Å | ||
|SITE= <scene name='pdbsite=AC1:Anp+Binding+Site+For+Chain+C'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Anp+Binding+Site+For+Chain+C'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER'>ANP</scene> | + | |LIGAND= <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2chq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2chq OCA], [http://www.ebi.ac.uk/pdbsum/2chq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2chq RCSB]</span> | ||
}} | }} | ||
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[[Category: Singleton, M R.]] | [[Category: Singleton, M R.]] | ||
[[Category: Wigley, D B.]] | [[Category: Wigley, D B.]] | ||
| - | [[Category: ANP]] | ||
[[Category: aaa+ atpase]] | [[Category: aaa+ atpase]] | ||
[[Category: atp-binding]] | [[Category: atp-binding]] | ||
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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 Mon Mar 31 02:21:37 2008'' |
Revision as of 23:21, 30 March 2008
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| , resolution 3.50Å | |||||||
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| Sites: | |||||||
| Ligands: | |||||||
| 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
2CHQ 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 Mon Mar 31 02:21:37 2008
