3zdr: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Structure of the Alcohol dehydrogenase (ADH) domain of a bifunctional ADHE dehydrogenase from Geobacillus thermoglucosidasius NCIMB 11955== | |||
<StructureSection load='3zdr' size='340' side='right' caption='[[3zdr]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3zdr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Geobacillus_thermoglucosidasius Geobacillus thermoglucosidasius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZDR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZDR FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3zdr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zdr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zdr RCSB], [http://www.ebi.ac.uk/pdbsum/3zdr PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Bifunctional alcohol/aldehyde dehydrogenase (ADHE) enzymes are found within many fermentative microorganisms. They catalyse the conversion of an acyl-coenzyme A to an alcohol via an aldehyde intermediate; this is coupled to the oxidation of two NADH molecules to maintain the NAD+ pool during fermentative metabolism. The structure of the alcohol dehydrogenase (ADH) domain of an ADHE protein from the ethanol-producing thermophile Geobacillus thermoglucosidasius has been determined to 2.5 A resolution. This is the first structure to be reported for such a domain. In silico modelling has been carried out to generate a homology model of the aldehyde dehydrogenase domain, and this was subsequently docked with the ADH-domain structure to model the structure of the complete ADHE protein. This model suggests, for the first time, a structural mechanism for the formation of the large multimeric assemblies or `spirosomes' that are observed for this ADHE protein and which have previously been reported for ADHEs from other organisms. | |||
Structure of a bifunctional alcohol dehydrogenase involved in bioethanol generation in Geobacillus thermoglucosidasius.,Extance J, Crennell SJ, Eley K, Cripps R, Hough DW, Danson MJ Acta Crystallogr D Biol Crystallogr. 2013 Oct 1;69(Pt 10):2104-2115. Epub 2013, Sep 20. PMID:24100328<ref>PMID:24100328</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Geobacillus thermoglucosidasius]] | [[Category: Geobacillus thermoglucosidasius]] | ||
[[Category: Crennell, S J | [[Category: Crennell, S J]] | ||
[[Category: Cripps, R | [[Category: Cripps, R]] | ||
[[Category: Danson, M J | [[Category: Danson, M J]] | ||
[[Category: Eley, K | [[Category: Eley, K]] | ||
[[Category: Extance, J | [[Category: Extance, J]] | ||
[[Category: Hough, D W | [[Category: Hough, D W]] | ||
[[Category: Bifunctional alcohol/aldehyde dehydrogenase]] | [[Category: Bifunctional alcohol/aldehyde dehydrogenase]] | ||
[[Category: Bioethanol]] | [[Category: Bioethanol]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
Revision as of 09:18, 4 January 2015
Structure of the Alcohol dehydrogenase (ADH) domain of a bifunctional ADHE dehydrogenase from Geobacillus thermoglucosidasius NCIMB 11955
| ||||||||||||
