3m9w | pdb_00003m9w

Open ligand-free crystal structure of xylose binding protein from Escherichia coli

spinqualitylabelsall models 3m9w, resolution 2.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3m9w is a 1 chain structure with sequence from Escherichia coli mg1655. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PO4 Related: 3m9x, 3ma0 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [XYLF_ECOLI] Involved in the high-affinity D-xylose membrane transport system. Binds with high affinity to xylose. 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 ATP binding cassette transport systems account for most import of necessary nutrients in bacteria. The periplasmic binding component (or an equivalent membrane-anchored protein) is critical to recognizing cognate ligand and directing it to the appropriate membrane permease. Here we report the X-ray structures of d-xylose binding protein from Escherichia coli in ligand-free open form, ligand-bound open form, and ligand-bound closed form at 2.15 A, 2.2 A, and 2.2 A resolutions, respectively. The ligand-bound open form is the first such structure to be reported at high resolution; the combination of the three different forms from the same protein furthermore gives unprecedented details concerning the conformational changes involved in binding protein function. As is typical of the structural family, the protein has two similar globular domains, which are connected by a three-stranded hinge region. The open liganded structure shows that xylose binds first to the C-terminal domain, with only very small conformational changes resulting. After a 34 degrees closing motion, additional interactions are formed with the N-terminal domain; changes in this domain are larger and serve to make the structure more ordered near the ligand. An analysis of the interactions suggests why xylose is the preferred ligand. Furthermore, a comparison with the most closely related proteins in the structural family shows that the conformational changes are distinct in each type of binding protein, which may have implications for how the individual proteins act in concert with their respective membrane permeases. Conformational Changes and Ligand Recognition of Escherichia colid-Xylose Binding Protein Revealed.,Sooriyaarachchi S, Ubhayasekera W, Park C, Mowbray SL J Mol Biol. 2010 Aug 1. PMID:20678502 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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