2CHG

Replication Factor C domains 1 and 2

Summary for 2CHG

• Entry DOI: 10.2210/pdb2chg/pdb
• Related: 2CHQ
• Descriptor: REPLICATION FACTOR C SMALL SUBUNIT, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: dna-binding protein, dna replication, clamp loader, aaa+ atpase, atp-binding, nucleotide-binding, dna binding protein
• Biological source: ARCHAEOGLOBUS FULGIDUS
• Total number of polymer chains: 4
• Total formula weight: 103642.91

Authors

Seybert, A.,Singleton, M.R.,Cook, N.,Hall, D.R.,Wigley, D.B. (deposition date: 2006-03-14, release date: 2006-06-06, Last modification date: 2024-05-08)

Primary citation

Seybert, A.,Singleton, M.R.,Cook, N.,Hall, D.R.,Wigley, D.B.
Communication between Subunits within an Archaeal Clamp-Loader Complex.
Embo J., 25:2209-, 2006

PubMed Abstract: 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.

PubMed: 16628222
DOI: 10.1038/SJ.EMBOJ.7601093

Experimental method

X-RAY DIFFRACTION (2.1 Å)