6QFP

Solution NMR ensemble for MlbQ at 298K compiled using the CoMAND method

6QFP の概要

• エントリーDOI: 10.2210/pdb6qfp/pdb
• NMR情報: BMRB: 25277
• 分子名称: Putative lipoprotein (1 entity in total)
• 機能のキーワード: comand method, r-factor refinement, signaling protein
• 由来する生物種: Microbispora sp. ATCC PTA-5024
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15456.09

構造登録者

ElGamacy, M.,Truffault, V.,Zhu, H.,Coles, M. (登録日: 2019-01-10, 公開日: 2019-04-10, 最終更新日: 2024-11-06)

主引用文献

ElGamacy, M.,Riss, M.,Zhu, H.,Truffault, V.,Coles, M.
Mapping Local Conformational Landscapes of Proteins in Solution.
Structure, 27:853-865.e5, 2019

PubMed Abstract: The ability of proteins to adopt multiple conformational states is essential to their function, and elucidating the details of such diversity under physiological conditions has been a major challenge. Here we present a generalized method for mapping protein population landscapes by NMR spectroscopy. Experimental NOESY spectra are directly compared with a set of expectation spectra back-calculated across an arbitrary conformational space. Signal decomposition of the experimental spectrum then directly yields the relative populations of local conformational microstates. In this way, averaged descriptions of conformation can be eliminated. As the method quantitatively compares experimental and expectation spectra, it inherently delivers an R factor expressing how well structural models explain the input data. We demonstrate that our method extracts sufficient information from a single 3D NOESY experiment to perform initial model building, refinement, and validation, thus offering a complete de novo structure determination protocol.

PubMed: 30930065
DOI: 10.1016/j.str.2019.03.005

実験手法

SOLUTION NMR