PMID:15205446

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Citation

Braun, V and Herrmann, C (2004) Point mutations in transmembrane helices 2 and 3 of ExbB and TolQ affect their activities in Escherichia coli K-12. J. Bacteriol. 186:4402-6

Abstract

Replacement of glutamate 176, the only charged amino acid in the third transmembrane helix of ExbB, with alanine (E176A) abolished ExbB activity in all determined ExbB-dependent functions of Escherichia coli. Combination of the mutations T148A in the second transmembrane helix and T181A in the third transmembrane helix, proposed to form part of a proton pathway through ExbB, also resulted in inactive ExbB. E176 and T148 are strictly conserved in ExbB and TolQ proteins, and T181 is almost strictly conserved in ExbB, TolQ, and MotA.

Links

PubMed PMC421596 Online version:10.1128/JB.186.13.4402-4406.2004

Keywords

Bacterial Proteins/physiology; Escherichia coli/physiology; Escherichia coli Proteins/genetics; Escherichia coli Proteins/physiology; Ferrichrome/metabolism; Point Mutation; Protein Structure, Secondary; Structure-Activity Relationship

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