Campus Units

Chemistry

Document Type

Article

Publication Version

Published Version

Publication Date

2015

Journal or Book Title

Proceedings of the National Academy of Sciences of the United States of America

Volume

112

Issue

37

First Page

11565

Last Page

11570

DOI

10.1073/pnas.1515366112

Abstract

The bacterial phosphotransferase system couples phosphoryl transfer to sugar transport across the cell membrane. The first protein in the pathway, Enzyme I (EI), undergoes two large rigid body domain reorientations between an autophosphorylation-competent closed state and an open state that allows subsequent phosphoryl transfer to its downstream protein partner. Simultaneous use of solution X-ray scattering and NMR dipolar coupling data to guide simulated annealing refinement reveals the existence of a dynamic equilibrium between closed and partially closed conformations in a complex of a mutant of EI with phosphoenolpyruvate. The partially closed conformation represents an intermediate in the open-to-closed transition.

Comments

This article is from Proceedings of the National Academy of Sciences of the United States of America 112 (2015): 11565, doi:10.1073/pnas.1515366112. Posted with permission

Rights

Works produced by employees of the U.S. Government as part of their official duties are not copyrighted within the U.S. The content of this document is not copyrighted.

Language

en

File Format

application/pdf

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