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1kev
From Proteopedia
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STRUCTURE OF NADP-DEPENDENT ALCOHOL DEHYDROGENASE
Overview
Two tetrameric NADP(+)-dependent bacterial secondary alcohol, dehydrogenases have been crystallized in the apo- and the holo-enzyme, forms. Crystals of the holo-enzyme from the mesophilic Clostridium, beijerinckii (NCBAD) belong to space group P2(1)2(1)2(1) with unit-cell, dimensions a = 90.5, b = 127.9, c = 151.4 A. Crystals of the apo-enzyme, (CBAD) belong to the same space group with unit-cell dimensions a = 80.4, b = 102.3, c = 193.5 A. Crystals of the holo-enzyme from the thermophilic, Thermoanaerobium brockii (NTBAD) belong to space group P6(1(5)) (a = b =, 80.6, c = 400.7 A). Crystals of the apo-form of TBAD (point mutant GI98D), belong to space group P2(1) with cell dimensions a = 123.0, b = 84.8, c =, 160.4 A beta = 99.5 degrees. Crystals of CBAD, NCBAD and NTBAD contain one, tetramer per asymmetric unit. They diffract to 2.0 A resolution at liquid, nitrogen temperature. Crystals of TBAD(GI98D) have two tetramers per, asymmetric unit and diffract to 2.7 A at 276 K. Self-rotation analysis, shows that both enzymes are tetramers of 222 symmetry.
About this Structure
1KEV is a Single protein structure of sequence from Clostridium beijerinckii with ZN and NDP as ligands. Active as Alcohol dehydrogenase (NADP(+)), with EC number 1.1.1.2 Structure known Active Sites: S1, S2, S3 and S4. Full crystallographic information is available from OCA.
Reference
Crystalline alcohol dehydrogenases from the mesophilic bacterium Clostridium beijerinckii and the thermophilic bacterium Thermoanaerobium brockii: preparation, characterization and molecular symmetry., Korkhin Y, Frolow F, Bogin O, Peretz M, Kalb AJ, Burstein Y, Acta Crystallogr D Biol Crystallogr. 1996 Jul 1;52(Pt 4):882-6. PMID:15299659
Page seeded by OCA on Mon Nov 5 13:35:29 2007
