2rml

Solution structure of the N-terminal soluble domains of Bacillus subtilis CopA

spinqualitylabelsall models 2rml, 25 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2rml is a 1 chain structure with sequence from Bacillus subtilis. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1oq3 Gene: copA (Bacillus subtilis) Resources: FirstGlance, OCA, RCSB, PDBsum Function [COPA_BACSU] Involved in copper export. 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 CopA, a P-type ATPase from Bacillus subtilis, plays a major role in the resistance of the cell to copper by effecting the export of the metal across the cytoplasmic membrane. The N-terminus of the protein features two soluble domains (a and b), that each contain a Cu(I)-binding motif, MTCAAC. We have generated a stable form of the wild-type two-domain protein, CopAab, and determined its solution structure. This was found to be similar to that reported previously for a higher stability S46V variant, with minor differences mostly confined to the Ser(46)-containing beta3-strand of domain a. Chemical-shift analysis demonstrated that the two Cu(I)-binding motifs, located at different ends of the protein molecule, are both able to participate in Cu(I) binding and that Cu(I) is in rapid exchange between protein molecules. Surprisingly, UV-visible and fluorescence spectroscopy indicate very different modes of Cu(I) binding below and above a level of 1 Cu(I) per protein, consistent with a major structural change occurring above 1 Cu(I) per CopAab. Analytical equilibrium centrifugation and gel filtration results show that this is a result of Cu(I)-mediated dimerization of the protein. The resulting species is highly luminescent, indicating the presence of a solvent-shielded Cu(I) cluster. Structure and Cu(I)-binding properties of the N-terminal soluble domains of Bacillus subtilis CopA.,Singleton C, Banci L, Ciofi-Baffoni S, Tenori L, Kihlken MA, Boetzel R, Le Brun NE Biochem J. 2008 May 1;411(3):571-9. PMID:18215122 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also ATPase

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