1yai

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[[Category: oxidoreductase]]
[[Category: oxidoreductase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:36:25 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 16:33:10 2007''

Revision as of 14:28, 30 October 2007


1yai, resolution 1.9Å

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X-RAY STRUCTURE OF A BACTERIAL COPPER,ZINC SUPEROXIDE DISMUTASE

Overview

Eukaryotic Cu,Zn superoxide dismutases (CuZnSODs) are antioxidant enzymes, remarkable for their unusually stable beta-barrel fold and dimer assembly, diffusion-limited catalysis, and electrostatic guidance of their free, radical substrate. Point mutations of CuZnSOD cause the fatal human, neurodegenerative disease amyotrophic lateral sclerosis. We determined and, analyzed the first crystallographic structure (to our knowledge) for, CuZnSOD from a prokaryote, Photobacterium leiognathi, a luminescent, symbiont of Leiognathid fish. This structure, exemplifying prokaryotic, CuZnSODs, shares the active-site ligand geometry and the topology of the, Greek key beta-barrel common to the eukaryotic CuZnSODs. However, the, beta-barrel elements recruited to form the dimer interface, the strategy, ... [(full description)]

About this Structure

1YAI is a [Single protein] structure of sequence from [Photobacterium leiognathi] with CU and ZN as [ligands]. Active as [Superoxide dismutase], with EC number [1.15.1.1]. Structure known Active Sites: CU1, CU2, CU3, ZN1, ZN2 and ZN3. Full crystallographic information is available from [OCA].

Reference

Novel dimeric interface and electrostatic recognition in bacterial Cu,Zn superoxide dismutase., Bourne Y, Redford SM, Steinman HM, Lepock JR, Tainer JA, Getzoff ED, Proc Natl Acad Sci U S A. 1996 Nov 12;93(23):12774-9. PMID:8917495

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