1h2b
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(New page: 200px<br /> <applet load="1h2b" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h2b, resolution 1.62Å" /> '''CRYSTAL STRUCTURE O...)
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Revision as of 17:07, 29 October 2007
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CRYSTAL STRUCTURE OF THE ALCOHOL DEHYDROGENASE FROM THE HYPERTHERMOPHILIC ARCHAEON AEROPYRUM PERNIX AT 1.65A RESOLUTION
Overview
The structure of the recombinant medium chain alcohol dehydrogenase (ADH), from the hyperthermophilic archaeon Aeropyrum pernix has been solved by, the multiple anomalous dispersion technique using the signal from the, naturally occurring zinc ions. The enzyme is a tetramer with 222 point, group symmetry. The ADH monomer is formed from a catalytic and a, cofactor-binding domain, with the overall fold similar to previously, solved ADH structures. The 1.62 A resolution A.pernix ADH structure is, that of the holo form, with the cofactor NADH bound into the cleft between, the two domains. The electron density found in the active site has been, interpreted to be octanoic acid, which has been shown to be an inhibitor, of the enzyme. This inhibitor is positioned with its carbonyl oxygen atom, ... [(full description)]
About this Structure
1H2B is a [Single protein] structure of sequence from [Aeropyrum pernix] with ZN, OCA and NAJ as [ligands]. Active as [[1]], with EC number [1.1.1.1]. Full crystallographic information is available from [OCA].
Reference
The structure of an alcohol dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix., Guy JE, Isupov MN, Littlechild JA, J Mol Biol. 2003 Aug 29;331(5):1041-51. PMID:12927540
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