4tm7 | pdb_00004tm7

Crystal structure of 6-phosphogluconolactonase from Mycobacterium smegmatis N131D mutant soaked with CuSO4

spinqualitylabelsall models 4tm7, resolution 1.39Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4tm7 is a 1 chain structure with sequence from Mycs2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, CU, CU1, EDO, SO4 Related: 4tm8 Gene: pgl, MSMEG_3099, MSMEI_3021 (MYCS2) Activity: 6-phosphogluconolactonase, with EC number 3.1.1.31 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed As an alternative to Darwinian evolution relying on catalytic promiscuity, a protein may acquire auxiliary function upon metal binding, thus providing it with a novel catalytic machinery. Here we show that addition of cupric ions to a 6-phosphogluconolactonase 6-PGLac bearing a putative metal binding site leads to the emergence of peroxidase activity (kcat 7.8 x 10(-2) s(-1), KM 1.1 x 10(-5) M). Both X-ray crystallographic and EPR data of the copper-loaded enzyme Cu.6-PGLac reveal a bis-histidine coordination site, located within a shallow binding pocket capable of accommodating the o-dianisidine substrate. Enzyme repurposing of a hydrolase as an emergent peroxidase upon metal binding.,Fujieda N, Schatti J, Stuttfeld E, Ohkubo K, Maier T, Fukuzumi S, Ward TR Chem Sci. 2015 Jul 1;6(7):4060-4065. doi: 10.1039/c5sc01065a. Epub 2015 May 7. PMID:29218172 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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