Weak and Transient Protein Interactions Determined by Solid-State NMR

被引：20

作者：

Dannatt, Hugh R. W. ^{[1
]}

Felletti, Michele ^{[1
]}

Jehle, Stefan ^{[1
]}

Wang, Yao ^{[2
]}

Emsley, Lyndon ^{[1
,3
]}

Dixon, Nicholas E. ^{[2
]}

Lesage, Anne ^{[1
]}

Pintacuda, Guido ^{[1
]}

机构：

[1] Univ Lyon, ENS Lyon, UCB Lyon 1, Ctr RMN Tres Hauts Champs,Inst Sci Analyt,CNRS, F-69100 Villeurbanne, France

[2] Univ Wollongong, Sch Chem, Ctr Med & Mol Biosci, Wollongong, NSW 2522, Australia

[3] Ecole Polytech Fed Lausanne, Inst Sci & Ingn Chim, CH-1015 Lausanne, Switzerland

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2016年 / 55卷 / 23期

基金：

澳大利亚研究理事会;

关键词：

DNA replication; magic angle spinning; solid-state NMR; protein structure; protein-protein interactions; SINGLE-STRANDED-DNA; ESCHERICHIA-COLI SSB; PROTON-DETECTED NMR; C-TERMINAL DOMAIN; BINDING-PROTEIN; BACKBONE ASSIGNMENT; MAS NMR; SPECTROSCOPY; RESOLUTION; DYNAMICS;

D O I：

10.1002/anie.201511609

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Despite their roles in controlling many cellular processes, weak and transient interactions between large structured macromolecules and disordered protein segments cannot currently be characterized at atomic resolution by Xray crystallography or solution NMR. Solid-state NMR does not suffer from the molecular size limitations affecting solution NMR, and it can be applied to molecules in different aggregation states, including non-crystalline precipitates and sediments. A solid-state NMR approach based on high magnetic fields, fast magic-angle sample spinning, and deuteration provides chemical-shift and relaxation mapping that enabled the characterization of the structure and dynamics of the transient association between two regions in an 80 kDa protein assembly. This led to direct verification of a mechanism of regulation of E. coli DNA metabolism.

引用

页码：6638 / 6641

页数：4

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