3ce1: Difference between revisions
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[[Category: Teh, A H]] | [[Category: Teh, A H]] | ||
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[[Category: Greek-key beta barrel]] | [[Category: Greek-key beta barrel]] | ||
[[Category: Metal-binding]] | [[Category: Metal-binding]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
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Revision as of 11:25, 25 October 2017
Crystal Structure of the Cu/Zn Superoxide Dismutase from Cryptococcus liquefaciens Strain N6Crystal Structure of the Cu/Zn Superoxide Dismutase from Cryptococcus liquefaciens Strain N6
Structural highlights
Function[A0ZPR9_9TREE] Destroys radicals which are normally produced within the cells and which are toxic to biological systems (By similarity).[RuleBase:RU000393] 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 PubMedThe deep-sea yeast Cryptococcus liquefaciens strain N6 shows high tolerance towards heavy metals, and can grow in the presence of high concentrations of copper ions. Enzymatic analysis indicated that copper ions induced the Cu/Zn superoxide dismutase activity of strain N6 (Cl-SOD1). In this study, the 1.2A resolution crystal structure of Cl-SOD1 has revealed several significant residue substitutions compared to the other Cu/Zn SODs. In the electrostatic loop, notably, His135 and Pro136 replace the well-conserved linear residues, while Thr133 substitutes a highly conserved glycine. The electrostatic loop has been shown to be involved in the copper uptake process, and these substitutions have caused an inward dragging of the turn region of the loop. As the introduction of proline and abolishment of glycine decrease loop flexibility, this structural reorganization may have helped stabilize the loop conformation, possibly resulting in more efficient copper uptake and a more stabilized copper-bound form. Structure of Cu/Zn superoxide dismutase from the heavy-metal-tolerant yeast Cryptococcus liquefaciens strain N6.,Teh AH, Kanamasa S, Kajiwara S, Kumasaka T Biochem Biophys Res Commun. 2008 Sep 26;374(3):475-8. Epub 2008 Jul 18. PMID:18640099[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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