2K5X

Chemical shift structure of COLICIN E9 DNASE domain with its cognate immunity protein IM9

2K5X の概要

• エントリーDOI: 10.2210/pdb2k5x/pdb
• 関連するPDBエントリー: 1emv 1fsj 1imq
• 分子名称: Colicin-E9 immunity protein, Colicin-E9 (2 entities in total)
• 機能のキーワード: colicin e9, immunity protein im9, bacteriocin immunity, plasmid, antibiotic, antimicrobial, bacteriocin, endonuclease, hydrolase, metal-binding, nuclease, zinc, immune system-hydrolase complex, immune system/hydrolase
• 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: 24712.52

構造登録者

Montalvao, R.W.,Cavalli, A.,Vendruscolo, M. (登録日: 2008-07-01, 公開日: 2008-12-09, 最終更新日: 2024-05-29)

主引用文献

Montalvao, R.W.,Cavalli, A.,Salvatella, X.,Blundell, T.L.,Vendruscolo, M.
Structure Determination of Protein-Protein Complexes Using NMR Chemical Shifts: Case of an Endonuclease Colicin-Immunity Protein Complex
J.Am.Chem.Soc., 130:15990-15996, 2008

PubMed Abstract: Nuclear magnetic resonance (NMR) spectroscopy provides a range of powerful techniques for determining the structures and the dynamics of proteins. The high-resolution determination of the structures of protein-protein complexes, however, is still a challenging problem for this approach, since it can normally provide only a limited amount of structural information at protein-protein interfaces. We present here the determination using NMR chemical shifts of the structure (PDB code 2K5X) of the cytotoxic endonuclease domain from bacterial toxin colicin (E9) in complex with its cognate immunity protein (Im9). In order to achieve this result, we introduce the CamDock method, which combines a flexible docking procedure with a refinement that exploits the structural information provided by chemical shifts. The results that we report thus indicate that chemical shifts can be used as structural restraints for the determination of the conformations of protein complexes that are difficult to obtain by more standard NMR approaches.

PubMed: 18980319

実験手法

SOLUTION NMR