1kb0
From Proteopedia
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'''Crystal Structure of Quinohemoprotein Alcohol Dehydrogenase from Comamonas testosteroni''' | '''Crystal Structure of Quinohemoprotein Alcohol Dehydrogenase from Comamonas testosteroni''' | ||
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[[Category: Oubrie, A.]] | [[Category: Oubrie, A.]] | ||
[[Category: Rozeboom, H J.]] | [[Category: Rozeboom, H J.]] | ||
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| - | [[Category: | + | [[Category: Cytochrome c]] |
| - | [[Category: | + | [[Category: Oxidoreductase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:31:21 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 19:31, 2 May 2008
Crystal Structure of Quinohemoprotein Alcohol Dehydrogenase from Comamonas testosteroni
Overview
Quinoprotein alcohol dehydrogenases are redox enzymes that participate in distinctive catabolic pathways that enable bacteria to grow on various alcohols as the sole source of carbon and energy. The x-ray structure of the quinohemoprotein alcohol dehydrogenase from Comamonas testosteroni has been determined at 1.44 A resolution. It comprises two domains. The N-terminal domain has a beta-propeller fold and binds one pyrroloquinoline quinone cofactor and one calcium ion in the active site. A tetrahydrofuran-2-carboxylic acid molecule is present in the substrate-binding cleft. The position of this oxidation product provides valuable information on the amino acid residues involved in the reaction mechanism and their function. The C-terminal domain is an alpha-helical type I cytochrome c with His(608) and Met(647) as heme-iron ligands. This is the first reported structure of an electron transfer system between a quinoprotein alcohol dehydrogenase and cytochrome c. The shortest distance between pyrroloquinoline quinone and heme c is 12.9 A, one of the longest physiological edge-to-edge distances yet determined between two redox centers. A highly unusual disulfide bond between two adjacent cysteines bridges the redox centers. It appears essential for electron transfer. A water channel delineates a possible pathway for proton transfer from the active site to the solvent.
About this Structure
1KB0 is a Single protein structure of sequence from Comamonas testosteroni. Full crystallographic information is available from OCA.
Reference
Crystal structure of quinohemoprotein alcohol dehydrogenase from Comamonas testosteroni: structural basis for substrate oxidation and electron transfer., Oubrie A, Rozeboom HJ, Kalk KH, Huizinga EG, Dijkstra BW, J Biol Chem. 2002 Feb 1;277(5):3727-32. Epub 2001 Nov 19. PMID:11714714 Page seeded by OCA on Fri May 2 22:31:21 2008
