Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: variation of common themes.
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.
Quiocho
F A
FA
Howard Hughes Medical Institute, Baylor College of Medicine, Houston, Texas 77030, USA.
Ledvina
P S
PS
D001419:Bacteria / Q000737:chemistry* / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D001693:Biological Transport, Active; D002352:Carrier Proteins / Q000737:chemistry* / Q000378:metabolism; D002633:Chemotaxis; D018360:Crystallography, X-Ray; D006090:Gram-Negative Bacteria / Q000737:chemistry*; D006860:Hydrogen Bonding; D008024:Ligands; D008958:Models, Molecular; D011487:Protein Conformation
D001426:Bacterial Proteins; D002352:Carrier Proteins; D008024:Ligands