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2KS0

Solution NMR structure of the Q251Q8_DESHY(21-82) protein from Desulfitobacterium Hafniense, Northeast Structural Genomics Consortium Target DhR8C

2KS0 の概要
エントリーDOI10.2210/pdb2ks0/pdb
NMR情報BMRB: 16656
分子名称Uncharacterized protein (1 entity in total)
機能のキーワードyabp family, desulfitobacterium hafniense, structural genomics, psi-2, protein structure initiative, northeast structural genomics consortium, nesg, unknown function
由来する生物種Desulfitobacterium hafniense
タンパク質・核酸の鎖数2
化学式量合計16004.41
構造登録者
主引用文献Yang, Y.,Ramelot, T.A.,McCarrick, R.M.,Ni, S.,Feldmann, E.A.,Cort, J.R.,Wang, H.,Ciccosanti, C.,Jiang, M.,Janjua, H.,Acton, T.B.,Xiao, R.,Everett, J.K.,Montelione, G.T.,Kennedy, M.A.
Combining NMR and EPR methods for homodimer protein structure determination.
J.Am.Chem.Soc., 132:11910-11913, 2010
Cited by
PubMed Abstract: There is a general need to develop more powerful and more robust methods for structural characterization of homodimers, homo-oligomers, and multiprotein complexes using solution-state NMR methods. In recent years, there has been increasing emphasis on integrating distinct and complementary methodologies for structure determination of multiprotein complexes. One approach not yet widely used is to obtain intermediate and long-range distance constraints from paramagnetic relaxation enhancements (PRE) and electron paramagnetic resonance (EPR)-based techniques such as double electron electron resonance (DEER), which, when used together, can provide supplemental distance constraints spanning to 10-70 A. In this Communication, we describe integration of PRE and DEER data with conventional solution-state nuclear magnetic resonance (NMR) methods for structure determination of Dsy0195, a homodimer (62 amino acids per monomer) from Desulfitobacterium hafniense. Our results indicate that combination of conventional NMR restraints with only one or a few DEER distance constraints and a small number of PRE constraints is sufficient for the automatic NMR-based structure determination program CYANA to build a network of interchain nuclear Overhauser effect constraints that can be used to accurately define both the homodimer interface and the global homodimer structure. The use of DEER distances as a source of supplemental constraints as described here has virtually no upper molecular weight limit, and utilization of the PRE constraints is limited only by the ability to make accurate assignments of the protein amide proton and nitrogen chemical shifts.
PubMed: 20698532
DOI: 10.1021/ja105080h
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 2ks0
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2026-04-15に公開中

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