2z22

Crystal structure of phosphate preplasmic binding protein psts from yersinia pestis

spinqualitylabelsall models 2z22, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2z22 is a 2 chain structure with sequence from Yersinia pestis co92. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PO4 Resources: FirstGlance, OCA, RCSB, PDBsum Function [Q7CFM9_YERPE] Part of the ABC transporter complex PstSACB involved in phosphate import (By similarity).[PIRNR:PIRNR002756] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Bacterial ATP-binding cassette (ABC) transport systems couple ATP hydrolysis with the uptake and efflux of a wide range of substances across bacterial membranes. These systems are comprised of transmembrane domains, nucleotide binding domains and, in the case of uptake systems, periplasmic binding proteins responsible for binding and presentation of substrate to the transmembrane domains. In pathogenic bacteria, ABC systems are known to play roles in virulence and pathogenicity and the surface localization of some components has made them attractive targets for both vaccine and anti-infective development. Here, the crystallization of five proteins (OppA, PstS, PiuA, YrbD and CysP) from Yersinia pestis, the causative agent of plague, are reported that diffracted to resolution limits ranging from 1.6 to 5 A. The first crystal structures of ABC system components from Y. pestis, OppA and PstS, are also reported here as complexes with their substrates. Comparisons of these two structures with known structures of related proteins suggest that these proteins possess versatility in substrate recognition and variations in protein-protein interactions with their cognate transmembrane domains. Structures of OppA and PstS from Yersinia pestis indicate variability of interactions with transmembrane domains.,Tanabe M, Mirza O, Bertrand T, Atkins HS, Titball RW, Iwata S, Brown KA, Byrne B Acta Crystallogr D Biol Crystallogr. 2007 Nov;63(Pt 11):1185-93. Epub 2007, Oct 17. PMID:18007034 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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