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4J2E

RB69 DNA Polymerase L415M Ternary Complex

4J2E の概要
エントリーDOI10.2210/pdb4j2e/pdb
関連するPDBエントリー4J2A 4J2B 4J2D
分子名称DNA polymerase, DNA (5'-D(*TP*CP*GP*TP*CP*TP*AP*AP*GP*CP*AP*GP*TP*CP*CP*GP*CP*G)-3'), DNA (5'-D(*GP*CP*GP*GP*AP*CP*TP*GP*CP*TP*TP*AP*G)-3'), ... (6 entities in total)
機能のキーワードrb69, dna polymerase, l415m, polymerase, transferase-dna complex, transferase/dna
由来する生物種Enterobacteria phage RB69
タンパク質・核酸の鎖数3
化学式量合計114658.73
構造登録者
Xia, S.,Wang, J.,Konigsberg, W.H. (登録日: 2013-02-04, 公開日: 2014-02-19, 最終更新日: 2024-02-28)
主引用文献Xia, S.,Wood, M.,Bradley, M.J.,De La Cruz, E.M.,Konigsberg, W.H.
Alteration in the cavity size adjacent to the active site of RB69 DNA polymerase changes its conformational dynamics.
Nucleic Acids Res., 41:9077-9089, 2013
Cited by
PubMed Abstract: Internal cavities are a common feature of many proteins, often having profound effects on the dynamics of their interactions with substrate and binding partners. RB69 DNA polymerase (pol) has a hydrophobic cavity right below the nucleotide binding pocket at the tip of highly conserved L415 side chain. Replacement of this residue with Gly or Met in other B family pols resulted in higher mutation rates. When similar substitutions for L415 were introduced into RB69pol, only L415A and L415G had dramatic effects on pre-steady-state kinetic parameters, reducing base selectivity by several hundred fold. On the other hand, the L415M variant behaved like the wild-type. Using a novel tC(o)-tCnitro Förster Resonance Energy Transfer (FRET) assay, we were able to show that the partition of the primer terminus between pol and exonuclease (exo) domains was compromised with the L415A and L415G mutants, but not with the L415M variant. These results could be rationalized by changes in their structures as determined by high resolution X-ray crystallography.
PubMed: 23921641
DOI: 10.1093/nar/gkt674
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.02 Å)
構造検証レポート
Validation report summary of 4j2e
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2024-11-27に公開中

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