1yai
From Proteopedia
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| - | [[Image:1yai. | + | [[Image:1yai.jpg|left|200px]]<br /><applet load="1yai" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1yai" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1yai, resolution 1.9Å" /> | caption="1yai, resolution 1.9Å" /> | ||
'''X-RAY STRUCTURE OF A BACTERIAL COPPER,ZINC SUPEROXIDE DISMUTASE'''<br /> | '''X-RAY STRUCTURE OF A BACTERIAL COPPER,ZINC SUPEROXIDE DISMUTASE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1YAI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Photobacterium_leiognathi Photobacterium leiognathi] with CU and ZN as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] | + | 1YAI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Photobacterium_leiognathi Photobacterium leiognathi] with CU and ZN as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] Known structural/functional Sites: <scene name='pdbsite=CU1:Cu Binding Site'>CU1</scene>, <scene name='pdbsite=CU2:Cu Binding Site'>CU2</scene>, <scene name='pdbsite=CU3:Cu Binding Site'>CU3</scene>, <scene name='pdbsite=ZN1:Zn Binding Site'>ZN1</scene>, <scene name='pdbsite=ZN2:Zn Binding Site'>ZN2</scene> and <scene name='pdbsite=ZN3:Zn Binding Site'>ZN3</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YAI OCA]. |
==Reference== | ==Reference== | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 18:41:04 2007'' |
Revision as of 16:31, 18 December 2007
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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, used to forge the channel for electrostatic recognition of superoxide, radical, and the connectivity of the intrasubunit disulfide bond in P., leiognathi CuZnSOD are discrete and strikingly dissimilar from those, highly conserved in eukaryotic CuZnSODs. This new CuZnSOD structure, broadens our understanding of structural features necessary and sufficient, for CuZnSOD activity, highlights a hitherto unrecognized adaptability of, the Greek key beta-barrel building block in evolution, and reveals that, prokaryotic and eukaryotic enzymes diverged from one primordial CuZnSOD, and then converged to distinct dimeric enzymes with electrostatic, substrate guidance.
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 Known structural/functional Sites: , , , , and . 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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