1q0f
|
Crystal structure of Ni-containing superoxide dismutase with Ni-ligation corresponding to the state after partial x-ray-induced reduction
OverviewOverview
Superoxide dismutases (SODs, EC 1.15.1.1) are ubiquitous enzymes that, efficiently catalyze the dismutation of superoxide radical anions to, protect biological molecules from oxidative damage. The crystal structure, of nickel-containing SOD (NiSOD) from Streptomyces seoulensis was, determined for the resting, x-ray-reduced, and thiosulfate-reduced enzyme, state. NiSOD is a homohexamer consisting of four-helix-bundle subunits., The catalytic center resides in the N-terminal active-site loop, where a, Ni(III) ion is coordinated by the amino group of His-1, the amide group of, Cys-2, two thiolate groups of Cys-2 and Cys-6, and the imidazolate of, His-1 as axial ligand that is lost in the chemically reduced state as well, as after x-ray-induced reduction. This structure represents a third class, of SODs concerning the catalytic metal species, subunit structure, and, oligomeric organization. It adds a member to the small number of, Ni-metalloenzymes and contributes with its Ni(III) active site to the, general understanding of Ni-related biochemistry. NiSOD is shown to occur, also in bacteria other than Streptomyces and is predicted to be present in, some cyanobacteria.
About this StructureAbout this Structure
1Q0F is a Single protein structure of sequence from Streptomyces seoulensis with SO4 and 3NI as ligands. Active as Superoxide dismutase, with EC number 1.15.1.1 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of nickel-containing superoxide dismutase reveals another type of active site., Wuerges J, Lee JW, Yim YI, Yim HS, Kang SO, Carugo KD, Proc Natl Acad Sci U S A. 2004 Jun 8;101(23):8569-74. Epub 2004 Jun 1. PMID:15173586
Page seeded by OCA on Wed Nov 21 00:16:45 2007