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Backbone resonance assignments for the ligand binding subunit of the histidine permease complex (HisJ) from Escherichia coli, under histidine-bound and unbound states

Backbone resonance assignments for the ligand binding subunit of the histidine permease complex... HisJ is a histidine binding subunit of the histidine permease, which exists in the outer membrane of Gram-negative bacteria. In order to incorporate the periplasmic histidine into the cell, HisJ captures histidine in the periplasm, and transfers the histidine to the transmembrane complex of histidine permease that is an ABC transporter. We established the backbone resonance assignments of 1H/13C/15N-labeled HisJ from Escherichia coli, in the histidine-bound and unbound states. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biomolecular NMR Assignments Springer Journals

Backbone resonance assignments for the ligand binding subunit of the histidine permease complex (HisJ) from Escherichia coli, under histidine-bound and unbound states

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References (15)

Publisher
Springer Journals
Copyright
Copyright © 2009 by Springer Science+Business Media B.V.
Subject
Physics; Biochemistry, general; Polymer Sciences ; Biophysics and Biological Physics
ISSN
1874-2718
eISSN
1874-270X
DOI
10.1007/s12104-009-9200-6
pmid
19921465
Publisher site
See Article on Publisher Site

Abstract

HisJ is a histidine binding subunit of the histidine permease, which exists in the outer membrane of Gram-negative bacteria. In order to incorporate the periplasmic histidine into the cell, HisJ captures histidine in the periplasm, and transfers the histidine to the transmembrane complex of histidine permease that is an ABC transporter. We established the backbone resonance assignments of 1H/13C/15N-labeled HisJ from Escherichia coli, in the histidine-bound and unbound states.

Journal

Biomolecular NMR AssignmentsSpringer Journals

Published: Nov 17, 2009

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