1ba9
From Proteopedia
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THE SOLUTION STRUCTURE OF REDUCED MONOMERIC SUPEROXIDE DISMUTASE, NMR, 36 STRUCTURES
Overview
Copper, zinc superoxide dismutase is a dimeric enzyme, and it has been, shown that no cooperativity between the two subunits of the dimer is, operative. The substitution of two hydrophobic residues, Phe 50 and Gly, 51, with two Glu's at the interface region has disrupted the quaternary, structure of the protein, thus producing a soluble monomeric form., However, this monomeric form was found to have an activity lower than that, of the native dimeric species (10%). To answer the fundamental question of, the role of the quaternary structure in the catalytic process of, superoxide dismutase, we have determined the solution structure of the, reduced monomeric mutant through NMR spectroscopy. Another fundamental, issue with respect to the enzymatic mechanism is the coordination of, reduced ... [(full description)]
About this Structure
1BA9 is a [Single protein] structure of sequence from [Homo sapiens] with ZN and CU1 as [ligands]. Active as [Superoxide dismutase], with EC number [1.15.1.1]. Structure known Active Sites: CU and ZN. Full crystallographic information is available from [OCA].
Reference
Solution structure of reduced monomeric Q133M2 copper, zinc superoxide dismutase (SOD). Why is SOD a dimeric enzyme?., Banci L, Benedetto M, Bertini I, Del Conte R, Piccioli M, Viezzoli MS, Biochemistry. 1998 Aug 25;37(34):11780-91. PMID:9718300
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