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[[Image:1ad3.gif|left|200px]]<br /><applet load="1ad3" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ad3, resolution 2.6&Aring;" />
'''CLASS 3 ALDEHYDE DEHYDROGENASE COMPLEX WITH NICOTINAMIDE-ADENINE-DINUCLEOTIDE'''<br />


==Overview==
==CLASS 3 ALDEHYDE DEHYDROGENASE COMPLEX WITH NICOTINAMIDE-ADENINE-DINUCLEOTIDE==
The first structure of an aldehyde dehydrogenase (ALDH) is described at 2.6 A resolution. Each subunit of the dimeric enzyme contains an NAD-binding domain, a catalytic domain and a bridging domain. At the interface of these domains is a 15 A long funnel-shaped passage with a 6 x 12 A opening leading to a putative catalytic pocket. A new mode of NAD binding, which differs substantially from the classic beta-alpha-beta binding mode associated with the 'Rossmann fold', is observed which we term the beta-alpha,beta mode. Sequence comparisons of the class 3 ALDH with other ALDHs indicate a similar polypeptide fold, novel NAD-binding mode and catalytic site for this family. A mechanism for enzymatic specificity and activity is postulated.
<StructureSection load='1ad3' size='340' side='right'caption='[[1ad3]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ad3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AD3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AD3 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ad3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ad3 OCA], [https://pdbe.org/1ad3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ad3 RCSB], [https://www.ebi.ac.uk/pdbsum/1ad3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ad3 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AL3A1_RAT AL3A1_RAT] ALDHs play a major role in the detoxification of alcohol-derived acetaldehyde. They are involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation. This protein preferentially oxidizes aromatic aldehyde substrates. It may play a role in the oxidation of toxic aldehydes.
== 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/ad/1ad3_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=1ad3 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1AD3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=NAD:'>NAD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Aldehyde_dehydrogenase_(NAD(P)(+)) Aldehyde dehydrogenase (NAD(P)(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.5 1.2.1.5] Known structural/functional Sites: <scene name='pdbsite=CTA:Catalytic+CYS'>CTA</scene> and <scene name='pdbsite=CTB:Catalytic+CYS'>CTB</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AD3 OCA].
*[[Aldehyde dehydrogenase 3D structures|Aldehyde dehydrogenase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
The first structure of an aldehyde dehydrogenase reveals novel interactions between NAD and the Rossmann fold., Liu ZJ, Sun YJ, Rose J, Chung YJ, Hsiao CD, Chang WR, Kuo I, Perozich J, Lindahl R, Hempel J, Wang BC, Nat Struct Biol. 1997 Apr;4(4):317-26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9095201 9095201]
[[Category: Large Structures]]
[[Category: Aldehyde dehydrogenase (NAD(P)(+))]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Liu Z-J]]
[[Category: Liu, Z J.]]
[[Category: Rose J]]
[[Category: Rose, J.]]
[[Category: Wang BC]]
[[Category: Wang, B C.]]
[[Category: NAD]]
[[Category: aromatic aldehyde]]
[[Category: nadp]]
[[Category: oxidoreductase]]
 
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