Dynamic equilibrium between closed and partially closed states of the bacterial Enzyme I unveiled by solution NMR and X-ray scattering

Venditti Vincenzo; Schwieters Charles D.; Grishaev AlexanderClore G. Marius

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Dynamic equilibrium between closed and partially closed states of the bacterial Enzyme I unveiled by solution NMR and X-ray scattering

机译：Dynamic equilibrium between closed and partially closed states of the bacterial Enzyme I unveiled by solution NMR and X-ray scattering

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Enzyme I (EI) is the first component in the bacterial phosphotransferase system, a signal transduction pathway in which phosphoryl transfer through a series of bimolecular protein-protein interactions is coupled to sugar transport across the membrane. EI is a multidomain, 128-kDa homodimer that has been shown to exist in two conformational states related to one another by two large (50-90 degrees) rigid body domain reorientations. The open conformation of apo EI allows phosphoryl transfer from His189 located in the N-terminal domain a/ beta (EIN alpha/beta) subdomain to the downstream protein partner bound to the EIN alpha subdomain. The closed conformation, observed in a trapped phosphoryl transfer intermediate, brings the EIN alpha/beta subdomain into close proximity to the C-terminal dimerization domain (EIC), thereby permitting in-line phosphoryl transfer from phosphoenolpyruvate (PEP) bound to EIC to His189. Here, we investigate the solution conformation of a complex of an active site mutant of EI (H189A) with PEP. Simulated annealing refinement driven simultaneously by solution small angle X-ray scattering and NMR residual dipolar coupling data demonstrates unambiguously that the EI(H189A)-PEP complex exists in a dynamic equilibrium between two approximately equally populated conformational states, one corresponding to the closed structure and the other to a partially closed species. The latter likely represents an intermediate in the open-to-closed transition.

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《Proceedings of the National Academy of Sciences of the United States of America》 |2015年第37期|11565-11570|共6页
作者
Venditti Vincenzo; Schwieters Charles D.; Grishaev AlexanderClore G. Marius;
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作者单位

NIDDK, Chem Phys Lab, NIH, Bethesda, MD 20892 USA;

NIH, Divis Computat Biosci, Ctr Informat Technol, Bethesda, MD 20892 USA;

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收录信息美国《科学引文索引》(SCI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
原文格式 PDF
正文语种英语
中图分类自然科学总论;
关键词
multidomain protein dynamics; dipolar couplings; X-ray scattering; conformational states; ligand binding;

Dynamic equilibrium between closed and partially closed states of the bacterial Enzyme I unveiled by solution NMR and X-ray scattering

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