1q0f: Difference between revisions

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{{STRUCTURE_1q0f|  PDB=1q0f  |  SCENE=  }}  
{{STRUCTURE_1q0f|  PDB=1q0f  |  SCENE=  }}  


'''Crystal structure of Ni-containing superoxide dismutase with Ni-ligation corresponding to the state after partial x-ray-induced reduction'''
===Crystal structure of Ni-containing superoxide dismutase with Ni-ligation corresponding to the state after partial x-ray-induced reduction===




==Overview==
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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.
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{{ABSTRACT_PUBMED_15173586}}


==About this Structure==
==About this Structure==
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[[Category: Yim, Y I.]]
[[Category: Yim, Y I.]]
[[Category: Homohexamer of four-helix bundle]]
[[Category: Homohexamer of four-helix bundle]]
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