2MV0

Solution NMR Structure of Maltose-binding protein from Escherichia coli, Northeast Structural Genomics Consortium (NESG) Target ER690

2MV0 の概要

• エントリーDOI: 10.2210/pdb2mv0/pdb
• 分子名称: Maltose-binding periplasmic protein (1 entity in total)
• 機能のキーワード: structural genomics, northeast structural genomics consortium, nesg, psi-biology, protein structure initiative, periplasmic binding protein
• 由来する生物種: Escherichia coli K-12
• 細胞内の位置: Periplasm: P0AEX9
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 40753.15

構造登録者

Rossi, P.,Lange, O.F.,Sgourakis, N.G.,Song, Y.,Lee, H.,Aramini, J.M.,Ertekin, A.,Xiao, R.,Acton, T.B.,Baker, D.,Montelione, G.T.,Northeast Structural Genomics Consortium (NESG) (登録日: 2014-09-18, 公開日: 2014-12-10, 最終更新日: 2024-05-15)

主引用文献

Lange, O.F.,Rossi, P.,Sgourakis, N.G.,Song, Y.,Lee, H.W.,Aramini, J.M.,Ertekin, A.,Xiao, R.,Acton, T.B.,Montelione, G.T.,Baker, D.
Determination of solution structures of proteins up to 40 kDa using CS-Rosetta with sparse NMR data from deuterated samples.
Proc.Natl.Acad.Sci.USA, 109:10873-10878, 2012

PubMed Abstract: We have developed an approach for determining NMR structures of proteins over 20 kDa that utilizes sparse distance restraints obtained using transverse relaxation optimized spectroscopy experiments on perdeuterated samples to guide RASREC Rosetta NMR structure calculations. The method was tested on 11 proteins ranging from 15 to 40 kDa, seven of which were previously unsolved. The RASREC Rosetta models were in good agreement with models obtained using traditional NMR methods with larger restraint sets. In five cases X-ray structures were determined or were available, allowing comparison of the accuracy of the Rosetta models and conventional NMR models. In all five cases, the Rosetta models were more similar to the X-ray structures over both the backbone and side-chain conformations than the "best effort" structures determined by conventional methods. The incorporation of sparse distance restraints into RASREC Rosetta allows routine determination of high-quality solution NMR structures for proteins up to 40 kDa, and should be broadly useful in structural biology.

PubMed: 22733734
DOI: 10.1073/pnas.1203013109

実験手法

SOLUTION NMR