1yai: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 5: | Line 5: | ||
==Overview== | ==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, ... | 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== | ==About this Structure== | ||
1YAI is a | 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] Structure known Active Sites: CU1, CU2, CU3, ZN1, ZN2 and ZN3. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YAI OCA]. | ||
==Reference== | ==Reference== | ||
| Line 27: | Line 27: | ||
[[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 Mon Nov 5 13:22:28 2007'' | ||
