1xtm

Crystal structure of the double mutant Y88H-P104H of a SOD-like protein from Bacillus subtilis.

spinqualitylabelsall models 1xtm, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1xtm is a 2 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.6Å Ligands: CU, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function YOJM_BACSU 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 It is known that several prokaryotic protein sequences, characterized by high homology with the eukaryotic Cu,ZnSODs, lack some of the metal ligands. In the present work, we have stepwise reintroduced the two missing copper ligands in the SOD-like protein of Bacillus subtilis, through site-directed mutagenesis. The mutant with three out of the four His that bind copper is not active, whereas the fully reconstituted mutant displays an activity of about 10% that of human Cu,ZnSOD. The mutated proteins have been characterized in solution and in the solid state. In solution, the proteins experience conformational disorder, which is believed to be partly responsible for the decreased enzymatic activity and sheds light on the tendency of several human SOD mutants to introduce mobility in the protein frame. In the crystal, on the contrary, the protein has a well-defined conformation, giving rise to dimers through the coordination of an exogenous zinc ion. The catalytic properties of the double mutant, which might be regarded as a step in an artificial evolution from a nonactive SOD to a fully functioning enzyme, are discussed on the basis of the structural and dynamical properties. From an inactive prokaryotic SOD homologue to an active protein through site-directed mutagenesis.,Banci L, Benvenuti M, Bertini I, Cabelli DE, Calderone V, Fantoni A, Mangani S, Migliardi M, Viezzoli MS J Am Chem Soc. 2005 Sep 28;127(38):13287-92. PMID:16173759 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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