2CHV
Replication Factor C ADPNP complex
2CHV の概要
エントリーDOI | 10.2210/pdb2chv/pdb |
関連するPDBエントリー | 2CHG 2CHQ |
分子名称 | REPLICATION FACTOR C SMALL SUBUNIT (1 entity in total) |
機能のキーワード | dna-binding protein, dna replication, clamp loader, aaa+ atpase, atp-binding, nucleotide-binding, dna binding protein |
由来する生物種 | ARCHAEOGLOBUS FULGIDUS |
タンパク質・核酸の鎖数 | 6 |
化学式量合計 | 216237.37 |
構造登録者 | Seybert, A.,Singleton, M.R.,Cook, N.,Hall, D.R.,Wigley, D.B. (登録日: 2006-03-16, 公開日: 2006-06-06, 最終更新日: 2024-05-08) |
主引用文献 | 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 Cited by 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: 16628222DOI: 10.1038/SJ.EMBOJ.7601093 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (4 Å) |
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