3hud
From Proteopedia
(New page: 200px<br /> <applet load="3hud" size="450" color="white" frame="true" align="right" spinBox="true" caption="3hud, resolution 3.2Å" /> '''THE STRUCTURE OF HUM...) |
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caption="3hud, resolution 3.2Å" /> | caption="3hud, resolution 3.2Å" /> | ||
'''THE STRUCTURE OF HUMAN BETA 1 BETA 1 ALCOHOL DEHYDROGENASE: CATALYTIC EFFECTS OF NON-ACTIVE-SITE SUBSTITUTIONS'''<br /> | '''THE STRUCTURE OF HUMAN BETA 1 BETA 1 ALCOHOL DEHYDROGENASE: CATALYTIC EFFECTS OF NON-ACTIVE-SITE SUBSTITUTIONS'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 3HUD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN and NAD 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] Full crystallographic information is available from [http:// | + | 3HUD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=NAD:'>NAD</scene> 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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HUD OCA]. |
==Reference== | ==Reference== | ||
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[[Category: oxidoreductase(nad(a)-choh(d))]] | [[Category: oxidoreductase(nad(a)-choh(d))]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:43:32 2008'' |
Revision as of 15:43, 15 February 2008
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THE STRUCTURE OF HUMAN BETA 1 BETA 1 ALCOHOL DEHYDROGENASE: CATALYTIC EFFECTS OF NON-ACTIVE-SITE SUBSTITUTIONS
Contents |
Overview
The three-dimensional structure of human beta 1 beta 1 alcohol, dehydrogenase (ADH; EC 1.1.1.1) complexed with NAD+ has been determined by, x-ray crystallography to 3.0-A resolution. The amino acids directly, involved in coenzyme binding are conserved between horse EE and human beta, 1 beta 1 alcohol dehydrogenase in all but one case [serine (horse) vs., threonine (human) at position 48]. As a result, the coenzyme molecule is, bound in a similar manner in the two enzymes. However, the strength of the, interactions in the vicinity of the pyrophosphate bridge of NAD+ appears, to be enhanced in the human enzyme. Side-chain movements of Arg-47 and, Asp-50 and a shift in the position of the helix comprising residues, 202-212 may explain both the decreased Vmax and the decreased rate of NADH, dissociation observed in the human enzyme vs. the horse enzyme. It appears, that these catalytic differences are not due to substitutions of any amino, acids directly involved in coenzyme binding but are the result of, structural rearrangements resulting from multiple sequence differences, between the two enzymes.
Disease
Known diseases associated with this structure: Alcoholism, susceptibility to OMIM:[103720]
About this Structure
3HUD is a Single protein structure of sequence from Homo sapiens with and as ligands. Active as Alcohol dehydrogenase, with EC number 1.1.1.1 Full crystallographic information is available from OCA.
Reference
Structure of human beta 1 beta 1 alcohol dehydrogenase: catalytic effects of non-active-site substitutions., Hurley TD, Bosron WF, Hamilton JA, Amzel LM, Proc Natl Acad Sci U S A. 1991 Sep 15;88(18):8149-53. PMID:1896463
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