3GLF
Crystal Structure of the Ecoli Clamp Loader Bound to Primer-Template DNA
3GLF の概要
| エントリーDOI | 10.2210/pdb3glf/pdb |
| 関連するPDBエントリー | 1JR3 1SXJ 1XXH 1XXI 3GLG 3GLH 3GLI |
| 分子名称 | DNA polymerase III subunit delta, DNA polymerase III subunit tau, DNA polymerase III subunit delta', ... (9 entities in total) |
| 機能のキーワード | aaa+ atpase, clamp loader, gamma complex, replication, dna replication, dna-directed dna polymerase, nucleotidyltransferase, transferase, atp-binding, nucleotide-binding, transferase-dna complex, transferase/dna |
| 由来する生物種 | Escherichia coli 詳細 |
| タンパク質・核酸の鎖数 | 14 |
| 化学式量合計 | 434033.51 |
| 構造登録者 | |
| 主引用文献 | Simonetta, K.R.,Kazmirski, S.L.,Goedken, E.R.,Cantor, A.J.,Kelch, B.A.,McNally, R.,Seyedin, S.N.,Makino, D.L.,O'Donnell, M.,Kuriyan, J. The mechanism of ATP-dependent primer-template recognition by a clamp loader complex. Cell(Cambridge,Mass.), 137:659-671, 2009 Cited by PubMed Abstract: Clamp loaders load sliding clamps onto primer-template DNA. The structure of the E. coli clamp loader bound to DNA reveals the formation of an ATP-dependent spiral of ATPase domains that tracks only the template strand, allowing recognition of both RNA and DNA primers. Unlike hexameric helicases, in which DNA translocation requires distinct conformations of the ATPase domains, the clamp loader spiral is symmetric and is set up to trigger release upon DNA recognition. Specificity for primed DNA arises from blockage of the end of the primer and accommodation of the emerging template along a surface groove. A related structure reveals how the psi protein, essential for coupling the clamp loader to single-stranded DNA-binding protein (SSB), binds to the clamp loader. By stabilizing a conformation of the clamp loader that is consistent with the ATPase spiral observed upon DNA binding, psi binding promotes the clamp-loading activity of the complex. PubMed: 19450514DOI: 10.1016/j.cell.2009.03.044 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3.388 Å) |
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