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2V1X

Crystal structure of human RECQ-like DNA helicase

2V1X の概要
エントリーDOI10.2210/pdb2v1x/pdb
分子名称ATP-DEPENDENT DNA HELICASE Q1, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (7 entities in total)
機能のキーワードdna strand annealing, mismatch repair, nucleotide-binding, dna-binding, nuclear protein, atpase, helicase, hydrolase, atp-binding
由来する生物種HOMO SAPIENS (HUMAN)
細胞内の位置Nucleus : P46063
タンパク質・核酸の鎖数2
化学式量合計136246.92
構造登録者
主引用文献Pike, A.C.W.,Shrestha, B.,Popuri, V.,Burgess-Brown, N.,Muzzolini, L.,Costantini, S.,Vindigni, A.,Gileadi, O.
Structure of the Human Recq1 Helicase Reveals a Putative Strand-Separation Pin.
Proc.Natl.Acad.Sci.USA, 106:1039-, 2009
Cited by
PubMed Abstract: RecQ-like helicases, which include 5 members in the human genome, are important in maintaining genome integrity. We present a crystal structure of a truncated form of the human RECQ1 protein with Mg-ADP. The truncated protein is active in DNA fork unwinding but lacks other activities of the full-length enzyme: disruption of Holliday junctions and DNA strand annealing. The structure of human RECQ1 resembles that of Escherichia coli RecQ, with some important differences. All structural domains are conserved, including the 2 RecA-like domains and the RecQ-specific zinc-binding and winged-helix (WH) domains. However, the WH domain is positioned at a different orientation from that of the E. coli enzyme. We identify a prominent beta-hairpin of the WH domain as essential for DNA strand separation, which may be analogous to DNA strand-separation features of other DNA helicases. This hairpin is significantly shorter in the E. coli enzyme and is not required for its helicase activity, suggesting that there are significant differences between the modes of action of RecQ family members.
PubMed: 19151156
DOI: 10.1073/PNAS.0806908106
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2 Å)
構造検証レポート
Validation report summary of 2v1x
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-10-30に公開中

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