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

Shunsuke Igarashi, Masanori Osawa, Shin Ichiro Ozawa, Ichio Shimada

Research output: Contribution to journalArticle

1 Citation (Scopus)

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.

Original languageEnglish
Pages (from-to)17-20
Number of pages4
JournalBiomolecular NMR Assignments
Volume4
Issue number1
DOIs
Publication statusPublished - 2010 Apr
Externally publishedYes

Fingerprint

Histidine
Escherichia coli
Ligands
Periplasm
ATP-Binding Cassette Transporters
Gram-Negative Bacteria
Bacteria
Bacteria histidine permease
Membranes

Keywords

  • ABC transporter
  • Apo HisJ
  • Histidine
  • Histidine permease
  • Holo HisJ

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry

Cite this

Backbone resonance assignments for the ligand binding subunit of the histidine permease complex (HisJ) from Escherichia coli, under histidine-bound and unbound states. / Igarashi, Shunsuke; Osawa, Masanori; Ozawa, Shin Ichiro; Shimada, Ichio.

In: Biomolecular NMR Assignments, Vol. 4, No. 1, 04.2010, p. 17-20.

Research output: Contribution to journalArticle

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