2XY8

Paramagnetic-based NMR structure of the complex between the N- terminal epsilon domain and the theta domain of the DNA polymerase III

2XY8 の概要

• エントリーDOI: 10.2210/pdb2xy8/pdb
• 関連するPDBエントリー: 1J53 1J54 1MGZ
• 分子名称: DNA POLYMERASE III SUBUNIT EPSILON, DNA POLYMERASE III SUBUNIT THETA, CALCIUM ION (3 entities in total)
• 機能のキーワード: transferase, docking, experimental restraints, haddock program
• 由来する生物種: ESCHERICHIA COLI; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 29643.07

構造登録者

Schmitz, C.,Bonvin, A.M.J.J. (登録日: 2010-11-16, 公開日: 2011-06-29, 最終更新日: 2024-05-15)

主引用文献

Schmitz, C.,Bonvin, A.M.J.J.
Protein-Protein Haddocking Using Exclusively Pseudocontact Shifts.
J.Biomol.NMR, 50:263-266, 2011

PubMed Abstract: In order to enhance the structure determination process of macromolecular assemblies by NMR, we have implemented long-range pseudocontact shift (PCS) restraints into the data-driven protein docking package HADDOCK. We demonstrate the efficiency of the method on a synthetic, yet realistic case based on the lanthanide-labeled N-terminal ε domain of the E. coli DNA polymerase III (ε186) in complex with the HOT domain. Docking from the bound form of the two partners is swiftly executed (interface RMSDs < 1 Å) even with addition of very large amount of noise, while the conformational changes of the free form still present some challenges (interface RMSDs in a 3.1-3.9 Å range for the ten lowest energy complexes). Finally, using exclusively PCS as experimental information, we determine the structure of ε186 in complex with the HOT-homologue θ subunit of the E. coli DNA polymerase III.

PubMed: 21626213
DOI: 10.1007/S10858-011-9514-4

実験手法

SOLUTION NMR