2h5y

Crystallographic structure of the Molybdate-Binding Protein of Xanthomonas citri at 1.7 Ang resolution bound to molybdate

spinqualitylabelsall models 2h5y, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2h5y is a 3 chain structure with sequence from Xanthomonas citri pv. citri str. 306. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.7Å Ligands: MOO, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MODA_XANAC Part of the ABC transporter complex ModABC involved in the transport of molybdenum into the cell (Probable). Binds molybdate and tungstate with high affinity in vitro (PubMed:16879982). 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 Xanthomonas axonopodis pv. citri ModA protein is the ABC periplasmic binding component responsible for the capture of molybdate. The protein was crystallized with sodium molybdate using the hanging-drop vapour-diffusion method in the presence of PEG or sulfate. X-ray diffraction data were collected to a maximum resolution of 1.7 A using synchrotron radiation. The crystal belongs to the orthorhombic space group C222(1), with unit-cell parameters a = 68.15, b = 172.14, c = 112.04 A. The crystal structure was solved by molecular-replacement methods and structure refinement is in progress. Crystallization, data collection and phasing of the molybdate-binding protein of the phytopathogen Xanthomonas axonopodis pv. citri.,Santacruz CP, Balan A, Ferreira LC, Barbosa JA Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Mar 1;62(Pt, 3):289-91. Epub 2006 Feb 24. PMID:16511325 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also ABC transporter 3D structures

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