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[[Image:2iuv.gif|left|200px]]
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{{STRUCTURE_2iuv|  PDB=2iuv  |  SCENE=  }}
'''CRYSTAL STRUCTURE OF N-QUINOL FORM OF AROMATIC AMINE DEHYDROGENASE (AADH) FROM ALCALIGENES FAECALIS, FORM B'''


==CRYSTAL STRUCTURE OF N-QUINOL FORM OF AROMATIC AMINE DEHYDROGENASE (AADH) FROM ALCALIGENES FAECALIS, FORM B==
<StructureSection load='2iuv' size='340' side='right'caption='[[2iuv]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2iuv]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Alcaligenes_faecalis Alcaligenes faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IUV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IUV 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]] 1.55&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TQQ:(S)-2-AMINO-3-(6,7-DIHYDRO-6-IMINO-7-OXO-1H-INDOL-3-YL)PROPANOIC+ACID'>TQQ</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=2iuv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iuv OCA], [https://pdbe.org/2iuv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iuv RCSB], [https://www.ebi.ac.uk/pdbsum/2iuv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iuv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AAUB_ALCFA AAUB_ALCFA] Oxidizes primary aromatic amines and, more slowly, some long-chain aliphatic amines, but not methylamine or ethylamine. Uses azurin as an electron acceptor to transfer electrons from the reduced tryptophylquinone cofactor.<ref>PMID:11495996</ref> <ref>PMID:16279953</ref> <ref>PMID:8188594</ref> <ref>PMID:16614214</ref>
== 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/iu/2iuv_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2iuv ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The quinoprotein aromatic amine dehydrogenase (AADH) uses a covalently bound tryptophan tryptophylquinone (TTQ) cofactor to oxidatively deaminate primary aromatic amines. Recent crystal structures have provided insight into the reductive half-reaction. In contrast, no atomic details are available for the oxidative half-reaction. The TTQ O7 hydroxyl group is protonated during reduction, but it is unclear how this proton can be removed during the oxidative half-reaction. Furthermore, compared with the electron transfer from the N-quinol form, electron transfer from the non-physiological O-quinol form to azurin is significantly slower. Here we report crystal structures of the O-quinol, N-quinol, and N-semiquinone forms of AADH. A comparison of oxidized and substrate reduced AADH species reveals changes in the TTQ-containing subunit, extending from residues in the immediate vicinity of the N-quinol to the putative azurin docking site, suggesting a mechanism whereby TTQ redox state influences interprotein electron transfer. In contrast, chemical reduction of the TTQ center has no significant effect on protein conformation. Furthermore, structural reorganization upon substrate reduction places a water molecule near TTQ O7 where it can act as proton acceptor. The structure of the N-semiquinone, however, is essentially similar to oxidized AADH. Surprisingly, in the presence of substrate a covalent N-semiquinone substrate adduct is observed. To our knowledge this is the first detailed insight into a complex, branching mechanism of quinone oxidation where significant structural reorganization upon reduction of the quinone center directly influences formation of the electron transfer complex and nature of the electron transfer process.


==Overview==
Atomic level insight into the oxidative half-reaction of aromatic amine dehydrogenase.,Roujeinikova A, Scrutton NS, Leys D J Biol Chem. 2006 Dec 29;281(52):40264-72. Epub 2006 Sep 27. PMID:17005560<ref>PMID:17005560</ref>
The quinoprotein aromatic amine dehydrogenase (AADH) uses a covalently bound tryptophan tryptophylquinone (TTQ) cofactor to oxidatively deaminate primary aromatic amines. Recent crystal structures have provided insight into the reductive half-reaction. In contrast, no atomic details are available for the oxidative half-reaction. The TTQ O7 hydroxyl group is protonated during reduction, but it is unclear how this proton can be removed during the oxidative half-reaction. Furthermore, compared with the electron transfer from the N-quinol form, electron transfer from the non-physiological O-quinol form to azurin is significantly slower. Here we report crystal structures of the O-quinol, N-quinol, and N-semiquinone forms of AADH. A comparison of oxidized and substrate reduced AADH species reveals changes in the TTQ-containing subunit, extending from residues in the immediate vicinity of the N-quinol to the putative azurin docking site, suggesting a mechanism whereby TTQ redox state influences interprotein electron transfer. In contrast, chemical reduction of the TTQ center has no significant effect on protein conformation. Furthermore, structural reorganization upon substrate reduction places a water molecule near TTQ O7 where it can act as proton acceptor. The structure of the N-semiquinone, however, is essentially similar to oxidized AADH. Surprisingly, in the presence of substrate a covalent N-semiquinone substrate adduct is observed. To our knowledge this is the first detailed insight into a complex, branching mechanism of quinone oxidation where significant structural reorganization upon reduction of the quinone center directly influences formation of the electron transfer complex and nature of the electron transfer process.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2IUV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Alcaligenes_faecalis Alcaligenes faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IUV OCA].
</div>
<div class="pdbe-citations 2iuv" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Atomic level insight into the oxidative half-reaction of aromatic amine dehydrogenase., Roujeinikova A, Scrutton NS, Leys D, J Biol Chem. 2006 Dec 29;281(52):40264-72. Epub 2006 Sep 27. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17005560 17005560]
*[[Aromatic amine dehydrogenase 3D structures|Aromatic amine dehydrogenase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Alcaligenes faecalis]]
[[Category: Alcaligenes faecalis]]
[[Category: Aralkylamine dehydrogenase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Leys D]]
[[Category: Leys, D.]]
[[Category: Roujeinikova A]]
[[Category: Roujeinikova, A.]]
[[Category: Scrutton N]]
[[Category: Scrutton, N.]]
[[Category: Oxidoreductase]]
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