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Article

Distinct roles of highly conserved charged residues at the MotA-FliG interface in bacterial flagellar motor rotation.

Journal of bacteriology - 1 Feb 2013

Morimoto Yusuke V, Nakamura Shuichi, Hiraoka Koichi D, Namba Keiichi, Minamino Tohru

Abstract excerpt

Electrostatic interactions between the stator protein MotA and the rotor protein FliG are important for bacterial flagellar motor rotation. Arg90 and Glu98 of MotA are required not only for torque generation but also for stator assembly around the rotor, but their actual roles remain unknown. Here we analyzed the roles of functionally important charged residues at the MotA-FliG interface in motor performance....

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Source

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Identifiers

PMID: 23161029
DOI: 10.1128/JB.01971-12
PMCID: PMC3554000

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Distinct roles of highly conserved charged residues at the MotA-FliG interface in bacterial flagellar motor rotation.PMID 23161029Read ↗

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