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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

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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.

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Acknowledgments

This work was supported in part by grants from the Japan New Energy and Industrial Technology Development Organization (NEDO) and the Ministry of Economy, Trade, and Industry (METI) (to I.S.), a Grant-in-Aid for Scientific Research on Priority Areas from the Japanese Ministry of Education, Culture, Sports, Science, and Technology (to M.O. and I.S.), and a grant from Takeda Science Foundation (to M.O.).

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Correspondence to Ichio Shimada.

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Igarashi, S., Osawa, M., Ozawa, Si. et al. Backbone resonance assignments for the ligand binding subunit of the histidine permease complex (HisJ) from Escherichia coli, under histidine-bound and unbound states. Biomol NMR Assign 4, 17–20 (2010). https://doi.org/10.1007/s12104-009-9200-6

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