2chg
Replication Factor C domains 1 and 2Replication Factor C domains 1 and 2
Structural highlights
FunctionRFCS_ARCFU Part of the RFC clamp loader complex which loads the PCNA sliding clamp onto DNA. The complex possesses DNA-dependent ATPase activity which is further stimulated by PCNA.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedWe 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. 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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