1EWQ
CRYSTAL STRUCTURE TAQ MUTS COMPLEXED WITH A HETERODUPLEX DNA AT 2.2 A RESOLUTION
1EWQ の概要
| エントリーDOI | 10.2210/pdb1ewq/pdb |
| 分子名称 | DNA (5'-D(*GP*CP*GP*AP*CP*GP*CP*TP*AP*GP*CP*GP*TP*GP*CP*GP*GP*CP*TP*CP*GP*TP*C)-3'), DNA (5'-D(*GP*GP*AP*CP*GP*AP*GP*CP*CP*GP*CP*CP*GP*CP*TP*AP*GP*CP*GP*TP*CP*G)-3'), DNA MISMATCH REPAIR PROTEIN MUTS, ... (6 entities in total) |
| 機能のキーワード | multiple domains of protein, mostly mixed alpha-beta structures, one domain is entirely helical, double stranded helix, replication-dna complex, replication/dna |
| 由来する生物種 | Thermus aquaticus |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 187444.87 |
| 構造登録者 | |
| 主引用文献 | Obmolova, G.,Ban, C.,Hsieh, P.,Yang, W. Crystal structures of mismatch repair protein MutS and its complex with a substrate DNA. Nature, 407:703-710, 2000 Cited by PubMed Abstract: DNA mismatch repair is critical for increasing replication fidelity in organisms ranging from bacteria to humans. MutS protein, a member of the ABC ATPase superfamily, recognizes mispaired and unpaired bases in duplex DNA and initiates mismatch repair. Mutations in human MutS genes cause a predisposition to hereditary nonpolyposis colorectal cancer as well as sporadic tumours. Here we report the crystal structures of a MutS protein and a complex of MutS with a heteroduplex DNA containing an unpaired base. The structures reveal the general architecture of members of the MutS family, an induced-fit mechanism of recognition between four domains of a MutS dimer and a heteroduplex kinked at the mismatch, a composite ATPase active site composed of residues from both MutS subunits, and a transmitter region connecting the mismatch-binding and ATPase domains. The crystal structures also provide a molecular framework for understanding hereditary nonpolyposis colorectal cancer mutations and for postulating testable roles of MutS. PubMed: 11048710DOI: 10.1038/35037509 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.2 Å) |
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