PMID:15489458
| Citation |
Ma, Q, Roy, F, Herrmann, S, Taylor, BL and Johnson, MS (2004) The Aer protein of Escherichia coli forms a homodimer independent of the signaling domain and flavin adenine dinucleotide binding. J. Bacteriol. 186:7456-9 |
|---|---|
| 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. |
| Links |
PubMed PMC523205 Online version:10.1128/JB.186.21.7456-7459.2004 |
| Keywords |
Carrier Proteins/chemistry; Carrier Proteins/metabolism; Cross-Linking Reagents; Dimerization; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; Flavin-Adenine Dinucleotide/metabolism; Gene Expression Regulation, Bacterial; Mutation; Protein Structure, Tertiary; Signal Transduction |
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