Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: variation of common themes.

Abstract:

:Crystallographic structure refinement at very high resolutions of a dozen periplasmic receptors has revealed that, though they have different sizes (26 to 60 kDa) and little sequence homology, they have high tertiary structure similarity. They consist of two distinct globular domains bisected by a cleft or groove wherein the ligand binds and is buried by a hinge-bending motion between the two domains. Structural analysis also reveals how hydrogen-bonding interactions can be tailored to a wide spectrum of specificity, ranging from the stringent specificity for phosphate and sulphate to the more loose specificity for peptides.

journal_name

Mol Microbiol

journal_title

Molecular microbiology

authors

Quiocho FA,Ledvina PS

doi

10.1111/j.1365-2958.1996.tb02484.x

subject

Has Abstract

pub_date

1996-04-01 00:00:00

pages

17-25

issue

1

eissn

0950-382X

issn

1365-2958

journal_volume

20

pub_type

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