View source for 1v59


==Crystal structure of yeast lipoamide dehydrogenase complexed with NAD+==
<StructureSection load='1v59' size='340' side='right' caption='[[1v59]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1v59]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V59 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1V59 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrolipoyl_dehydrogenase Dihydrolipoyl dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.4 1.8.1.4] </span></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=1v59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v59 OCA], [http://pdbe.org/1v59 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1v59 RCSB], [http://www.ebi.ac.uk/pdbsum/1v59 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1v59 ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/DLDH_YEAST DLDH_YEAST]] Lipoamide dehydrogenase is a component of the alpha-ketoacid dehydrogenase complexes. This includes the pyruvate dehydrogenase complex, which catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). Acts also as component of the glycine cleavage system (glycine decarboxylase complex), which catalyzes the degradation of glycine. 
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v5/1v59_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1v59 ConSurf].
<div style="clear:both"></div>

==See Also==
*[[Dihydrolipoamide dehydrogenase|Dihydrolipoamide dehydrogenase]]
__TOC__
</StructureSection>
[[Category: Dihydrolipoyl dehydrogenase]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Adachi, W]]
[[Category: Reed, L J]]
[[Category: Sekiguchi, T]]
[[Category: Suzuki, K]]
[[Category: Takenaka, A]]
[[Category: Tsunoda, M]]
[[Category: 2-oxoacid dehydroganese complex]]
[[Category: Dihydrolipoamide dehydrogenase]]
[[Category: Lipoamide dehydrogenase]]
[[Category: Nad+]]
[[Category: Oxidoreductase]]
[[Category: Pyridine nucleotide-disulphide oxidoreductase]]
[[Category: Pyruvate dehydrogenase complex]]