1J53

Structure of the N-terminal Exonuclease Domain of the Epsilon Subunit of E.coli DNA Polymerase III at pH 8.5

1J53 の概要

• エントリーDOI: 10.2210/pdb1j53/pdb
• 関連するPDBエントリー: 1J54
• 分子名称: DNA polymerase III, epsilon chain, MANGANESE (II) ION, THYMIDINE-5'-PHOSPHATE, ... (5 entities in total)
• 機能のキーワード: dna polymerase proofreading domain, transferase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21620.12

構造登録者

Hamdan, S.,Carr, P.D.,Brown, S.E.,Ollis, D.L.,Dixon, N.E. (登録日: 2002-01-22, 公開日: 2002-10-16, 最終更新日: 2024-12-25)

主引用文献

Hamdan, S.,Carr, P.D.,Brown, S.E.,Ollis, D.L.,Dixon, N.E.
Structural Basis for Proofreading during Replication of the Escherichia coli Chromosome
Structure, 10:535-546, 2002

PubMed Abstract: The epsilon subunit of the Escherichia coli replicative DNA polymerase III is the proofreading 3'-5' exonuclease. Structures of its catalytic N-terminal domain (epsilon186) were determined at two pH values (5.8 and 8.5) at resolutions of 1.7-1.8 A, in complex with two Mn(II) ions and a nucleotide product of its reaction, thymidine 5'-monophosphate. The protein structure is built around a core five-stranded beta sheet that is a common feature of members of the DnaQ superfamily. The structures were identical, except for differences in the way TMP and water molecules are coordinated to the binuclear metal center in the active site. These data are used to develop a mechanism for epsilon and to produce a plausible model of the complex of epsilon186 with DNA.

PubMed: 11937058
DOI: 10.1016/S0969-2126(02)00738-4

実験手法

X-RAY DIFFRACTION (1.8 Å)