Backbone resonance assignments for the ligand binding subunit of the histidine permease complex (HisJ) from Escherichia coli, under histidine-bound and unbound states.
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 (1)H/(13)C/(15)N-labeled HisJ from Escherichia coli, in the histidine-bound and unbound states.
Igarashi
Shunsuke
S
Graduate School of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.
Osawa
Masanori
M
Ozawa
Shin-Ichiro
S
Shimada
Ichio
I
D000595:Amino Acid Sequence; D002247:Carbon Isotopes / Q000737:chemistry; D004926:Escherichia coli; D006657:Histones / Q000737:chemistry; D006859:Hydrogen / Q000737:chemistry; D009587:Nitrogen Isotopes / Q000737:chemistry; D019906:Nuclear Magnetic Resonance, Biomolecular; D033902:Periplasmic Binding Proteins / Q000737:chemistry* / Q000235:genetics
D002247:Carbon Isotopes; D006657:Histones; D009587:Nitrogen Isotopes; D033902:Periplasmic Binding Proteins; C018963:histidine-binding protein; D006859:Hydrogen