1a55

PHOSPHATE-BINDING PROTEIN MUTANT A197C

spinqualitylabelsall models 1a55, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1a55 is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.4Å Ligands: 2HP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PSTS_ECOLI Part of the ABC transporter complex PstSACB involved in phosphate import. 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 Crystal structures are presented for the A197C mutant of Escherichia coli phosphate binding protein (PBP) and the same mutant labeled at Cys197 with N-[2-(1-maleimidyl)ethyl]-7-(diethylamino)coumarin-3-carboxamide (MDCC). Both proteins are complexed with inorganic phosphate. The latter molecule, MDCC-PBP, exhibits a large increase in fluorescence on binding inorganic phosphate. The resulting high-fluorescence state of the coumarin and the ability of this coumarin to monitor the conformational changes associated with inorganic phosphate binding are interpreted in terms of the specific interactions of MDCC with the protein. The structure helps to explain why this particular label gives a high-fluorescence state on binding inorganic phosphate, while several other related labels do not, and hence aids our general understanding of environmentally sensitive fluorescence probes on proteins. Crystal structure of phosphate binding protein labeled with a coumarin fluorophore, a probe for inorganic phosphate.,Hirshberg M, Henrick K, Haire LL, Vasisht N, Brune M, Corrie JE, Webb MR Biochemistry. 1998 Jul 21;37(29):10381-5. PMID:9671506 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Phosphate-binding protein

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