Structure and dynamics of Escherichia coli chemosensory receptors. Engineered sulfhydryl studies.

Abstract:

:Cysteine residues introduced by site-directed mutagenesis have been used to probe the conformation and dynamics of two receptors in the E. coli chemotaxis pathway. (a) Thermal motions of the polypeptide backbone were investigated in the periplasmic D-galactose and D-glucose receptor, a globular protein of known structure. Disulfide bond formation between pairs of engineered sulfhydryls were used to trap collisions during the relative motions of surface alpha-helices I and X. Motions with amplitudes ranging from 4.5 to 15.2 A were detected on timescales ranging from 10(-4) to 10(-1) s, respectively. These results suggest that thermal backbone motions may have larger amplitudes than previously thought. (b) Conformational features of the transmembrane aspartate transducer have been investigated. Engineered sulfhydryls were used to ascertain the location and orientations of two putative transmembrane alpha-helices in the primary structure, to investigate the packing of these helices, to determine the oligomer and surface structures, and to detect thermal and ligand-induced dynamics of the polypeptide backbone. A model for the folded conformation of the transducer oligomer is reviewed.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Careaga CL,Falke JJ

doi

10.1016/S0006-3495(92)81806-4

subject

Has Abstract

pub_date

1992-04-01 00:00:00

pages

209-16; discussion 217-9

issue

1

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(92)81806-4

journal_volume

62

pub_type

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