2IDO

Structure of the E. coli Pol III epsilon-Hot proofreading complex

2IDO の概要

• エントリーDOI: 10.2210/pdb2ido/pdb
• 分子名称: DNA polymerase III epsilon subunit, Hot protein, MANGANESE (II) ION, ... (6 entities in total)
• 機能のキーワード: polymerase, exonuclease, hot, epsilon, pol iii, transferase
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 61884.49

構造登録者

Kirby, T.W.,Harvey, S.,DeRose, E.F.,Chalov, S.,Chikova, A.K.,Perrino, F.W.,Schaaper, R.M.,London, R.E.,Pedersen, L.C. (登録日: 2006-09-15, 公開日: 2006-11-14, 最終更新日: 2023-08-30)

主引用文献

Kirby, T.W.,Harvey, S.,DeRose, E.F.,Chalov, S.,Chikova, A.K.,Perrino, F.W.,Schaaper, R.M.,London, R.E.,Pedersen, L.C.
Structure of the Escherichia coli DNA polymerase III epsilon-HOT proofreading complex.
J.Biol.Chem., 281:38466-38471, 2006

PubMed Abstract: The epsilon subunit of Escherichia coli DNA polymerase III possesses 3'-exonucleolytic proofreading activity. Within the Pol III core, epsilon is tightly bound between the alpha subunit (DNA polymerase) and subunit. Here, we present the crystal structure of epsilon in complex with HOT, the bacteriophage P1-encoded homolog of , at 2.1 A resolution. The epsilon-HOT interface is defined by two areas of contact: an interaction of the previously unstructured N terminus of HOT with an edge of the epsilon central beta-sheet as well as interactions between HOT and the catalytically important helix alpha1-loop-helix alpha2 motif of epsilon. This structure provides insight into how HOT and, by implication, may stabilize the epsilon subunit, thus promoting efficient proofreading during chromosomal replication.

PubMed: 16973612
DOI: 10.1074/jbc.M606917200

実験手法

X-RAY DIFFRACTION (2.1 Å)