The Aer Protein of Escherichia coli Forms a Homodimer Independent of the Signaling Domain and Flavin Adenine Dinucleotide Binding-Reference-Cited by-同舟云学术

The Aer Protein of Escherichia coli Forms a Homodimer Independent of the Signaling Domain and Flavin Adenine Dinucleotide Binding

Published:2004-11 Issue:21 Volume:186 Page:7456-7459
ISSN:0021-9193
Container-title:Journal of Bacteriology
language:en
Short-container-title:J Bacteriol

Author:

Ma Qinhong¹,Roy Francis¹,Herrmann Sarah¹,Taylor Barry L.¹,Johnson Mark S.¹

Affiliation:

1. Division of Microbiology and Molecular Genetics, Loma Linda University, Loma Linda, California

Abstract

ABSTRACT In vivo cross-linking between native cysteines in the Aer receptor of Escherichia coli showed dimer formation at the membrane anchor and in the putative HAMP domain. Dimers also formed in mutants that did not bind flavin adenine dinucleotide and in truncated peptides without a signaling domain and part of the HAMP domain.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Link

https://journals.asm.org/doi/pdf/10.1128/JB.186.21.7456-7459.2004

Reference21 articles.

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