1h2b
From Proteopedia
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==Overview== | ==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, ... | + | 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, forming the fourth ligand of the catalytic zinc ion. The structural zinc, ion of each monomer is present at only partial occupancy and in its, absence a disulfide bond is formed. The enhanced thermal stability of the, A.pernix ADH is thought to arise primarily from increased ionic and, hydrophobic interactions on the subunit interfaces. |
==About this Structure== | ==About this Structure== | ||
| - | 1H2B is a | + | 1H2B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aeropyrum_pernix Aeropyrum pernix] with ZN, OCA and NAJ as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alcohol_dehydrogenase Alcohol dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.1 1.1.1.1] Structure known Active Site: OC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H2B OCA]. |
==Reference== | ==Reference== | ||
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[[Category: zinc]] | [[Category: zinc]] | ||
| - | ''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 13:56:50 2007'' |
Revision as of 11:51, 5 November 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, forming the fourth ligand of the catalytic zinc ion. The structural zinc, ion of each monomer is present at only partial occupancy and in its, absence a disulfide bond is formed. The enhanced thermal stability of the, A.pernix ADH is thought to arise primarily from increased ionic and, hydrophobic interactions on the subunit interfaces.
About this Structure
1H2B is a Single protein structure of sequence from Aeropyrum pernix with ZN, OCA and NAJ as ligands. Active as Alcohol dehydrogenase, with EC number 1.1.1.1 Structure known Active Site: OC1. 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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