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Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: variation of common themes
Author(s) -
Quiocho Florante A.,
Ledvina Polly S.
Publication year - 1996
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1996.tb02484.x
Subject(s) - periplasmic space , biology , chemotaxis , peptidoglycan , structural similarity , sequence alignment , homology (biology) , receptor , globular protein , protein structure , peptide sequence , crystallography , biophysics , computational biology , biochemistry , amino acid , escherichia coli , enzyme , chemistry , gene
Summary Crystallographic structure refinement at very high resolutions of a dozen periplasmic receptors has revealed that, though they have different sizes (26 to 60kDa) 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.