Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form

Mapping of the binding interfaces of the proteins of the bacterial phosphotransferase system, hpr and iia(glc)

Academic Article
uri icon
  • Overview
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Chen, Y.
  • Reizer, J.
  • Saier, M. H.
  • Fairbrother, W. J.
  • Wright, Peter

publication date

  • January 1993

journal

  • Biochemistry  Journal

abstract

  • Enzyme IIAglc and HPr are central regulatory and phosphocarrier proteins of the phosphoenolpyruvate:sugar phosphotransferase system (PTS) of bacteria. During phosphoryl transfer from phosphoenolpyruvate to glucose, phosphate is transferred from HPr to enzyme IIAglc. In order to characterize the binding interfaces of the two proteins during phosphate transfer, 15N-edited and 15N-filtered NMR experiments have been recorded for the complex of enzyme IIAglc and HPr from Bacillus subtilis. Uniformly 15N-labeled enzyme IIAglc and nonlabeled HPr were used in these studies. Residues which undergo significant chemical shift changes upon complex formation have been identified for both proteins. The binding interfaces of the two proteins, suggested by the observed chemical shift changes, involve predominantly hydrophobic surfaces near the active site His-15 of HPr and the phosphoryl acceptor His-83 of IIAglc.

subject areas

  • Bacillus subtilis
  • Bacterial Proteins
  • Binding Sites
  • Chemistry, Physical
  • Escherichia coli
  • Histidine
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Molecular Structure
  • Phosphoenolpyruvate Sugar Phosphotransferase System
  • Physicochemical Phenomena
  • Protein Structure, Secondary
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 0006-2960

Digital Object Identifier (DOI)

  • 10.1021/bi00052a006

PubMed ID

  • 8418852
scroll to property group menus

Additional Document Info

start page

  • 32

end page

  • 37

volume

  • 32

issue

  • 1

©2021 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support