2N9L

1H, 13C, and 15N Chemical Shift Assignments for in-cell GB1

2N9L の概要

• エントリーDOI: 10.2210/pdb2n9l/pdb
• 関連するPDBエントリー: 2N9K
• NMR情報: BMRB: 25910
• 分子名称: Immunoglobulin G-binding protein G (1 entity in total)
• 機能のキーワード: in-cell nmr, qme data processing, flya automatic assignment, bayesian, immune system
• 由来する生物種: Streptococcus sp. 'group G'
• 細胞内の位置: Secreted, cell wall ; Peptidoglycan-anchor : P19909
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 6258.84

構造登録者

Ikeya, T.,Hanashima, T.,Hosoya, S.,Shimazaki, M.,Ikeda, S.,Mishima, M.,Guentert, P.,Ito, Y. (登録日: 2015-11-30, 公開日: 2016-12-28, 最終更新日: 2024-05-15)

主引用文献

Ikeya, T.,Hanashima, T.,Hosoya, S.,Shimazaki, M.,Ikeda, S.,Mishima, M.,Guentert, P.,Ito, Y.
Improved in-cell structure determination of proteins at near-physiological concentration
Sci Rep, 6:38312-38312, 2016

PubMed Abstract: Investigating three-dimensional (3D) structures of proteins in living cells by in-cell nuclear magnetic resonance (NMR) spectroscopy opens an avenue towards understanding the structural basis of their functions and physical properties under physiological conditions inside cells. In-cell NMR provides data at atomic resolution non-invasively, and has been used to detect protein-protein interactions, thermodynamics of protein stability, the behavior of intrinsically disordered proteins, etc. in cells. However, so far only a single de novo 3D protein structure could be determined based on data derived only from in-cell NMR. Here we introduce methods that enable in-cell NMR protein structure determination for a larger number of proteins at concentrations that approach physiological ones. The new methods comprise (1) advances in the processing of non-uniformly sampled NMR data, which reduces the measurement time for the intrinsically short-lived in-cell NMR samples, (2) automatic chemical shift assignment for obtaining an optimal resonance assignment, and (3) structure refinement with Bayesian inference, which makes it possible to calculate accurate 3D protein structures from sparse data sets of conformational restraints. As an example application we determined the structure of the B1 domain of protein G at about 250 μM concentration in living E. coli cells.

PubMed: 27910948
DOI: 10.1038/srep38312

実験手法

SOLUTION NMR