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5KFT

Human DNA polymerase eta R61A-DNA ternary complex: reaction with 1 mM Mg2+ for 40s

5KFT の概要
エントリーDOI10.2210/pdb5kft/pdb
関連するPDBエントリー5KFA 5KFB 5KFC 5KFD 5KFE 5KFF 5KFG 5KFH 5KFI 5KFJ 5KFK 5KFL 5KFM 5KFN 5KFO 5KFP 5KFQ 5KFR 5KFS 5KFU 5KFV 5KFW 5KFX 5KFY 5KFZ 5KG0 5KG1 5KG2 5KG3 5KG4 5KG5 5KG6 5KG7
分子名称DNA polymerase eta, DNA (5'-D(*CP*AP*TP*TP*AP*TP*GP*AP*CP*GP*CP*T)-3'), DNA (5'-D(*AP*GP*CP*GP*TP*CP*AP*T)-3'), ... (9 entities in total)
機能のキーワードin crystallo reaction, dna polymerase, metal ion dependent catalysis, replication, transferase-dna complex, transferase/dna
由来する生物種Homo sapiens (Human)
詳細
タンパク質・核酸の鎖数3
化学式量合計55398.75
構造登録者
Gao, Y.,Yang, W. (登録日: 2016-06-12, 公開日: 2016-06-22, 最終更新日: 2023-09-27)
主引用文献Gao, Y.,Yang, W.
Capture of a third Mg2+ is essential for catalyzing DNA synthesis.
Science, 352:1334-1337, 2016
Cited by
PubMed Abstract: It is generally assumed that an enzyme-substrate (ES) complex contains all components necessary for catalysis and that conversion to products occurs by rearrangement of atoms, protons, and electrons. However, we find that DNA synthesis does not occur in a fully assembled DNA polymerase-DNA-deoxynucleoside triphosphate complex with two canonical metal ions bound. Using time-resolved x-ray crystallography, we show that the phosphoryltransfer reaction takes place only after the ES complex captures a third divalent cation that is not coordinated by the enzyme. Binding of the third cation is incompatible with the basal ES complex and requires thermal activation of the ES for entry. It is likely that the third cation provides the ultimate boost over the energy barrier to catalysis of DNA synthesis.
PubMed: 27284197
DOI: 10.1126/science.aad9633
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.52 Å)
構造検証レポート
Validation report summary of 5kft
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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