Structural similarities between the aspartate receptor of bacterial chemotaxis and the trp repressor of E. coli Implications for transmembrane signaling

FEBS Letters

Lynch, Berkley A.¹  Koshland, Daniel E.¹ 

[1] Department of Molecular and Cell Biology, 401 Barker Hall, University of California, Berkeley, CA 94720, USA

关键词: Aspartate receptor;    transmembrane signaling;    Tryptophan repressor;    Chemotaxis;   

DOI  :  10.1016/0014-5793(92)80891-J

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A high resolution structure of the N-terminal ligand-binding domain of the aspartate receptor which mediates aspartate chemotaxis in Salmonella typhimurium has recently been reported. A least-squares superposition of the α-amino nitrogen, α-carbon, β-carbon, and α-carboxylate carbon of the aspartate bound to the aspartate receptor onto the equivalent atoms in the tryptophan bound to the trp repressor provides evidence for similarity between key parts of the active sites that bind to the α-amino and α-carboxylates of the respective ligands. Because the N-terminal domain of the aspartate receptor and the trp repressor also share other structural similarities, we hypothesize that the similarity between the aspartate receptor and the trp repressor derives from a similarity in ligand-induced conformational changes at the active sites of these proteins. This hypothesis also implies that an important signaling event in the aspartate receptor occurs through tertiary conformational changes within a single subunit.

【 授权许可】

Unknown