View source for 1mae

==The Active Site Structure of Methylamine Dehydrogenase: Hydrazines Identify C6 as the Reactive Site of the Tryptophan Derived Quinone Cofactor==
<StructureSection load='1mae' size='340' side='right' caption='[[1mae]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1mae]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_25364 Atcc 25364]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MAE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MAE FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HDZ:NITROGEN+MOLECULE'>HDZ</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=0AF:7-HYDROXY-L-TRYPTOPHAN'>0AF</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methylamine_dehydrogenase_(amicyanin) Methylamine dehydrogenase (amicyanin)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.9.1 1.4.9.1] </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=1mae FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mae OCA], [http://pdbe.org/1mae PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mae RCSB], [http://www.ebi.ac.uk/pdbsum/1mae PDBsum]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/DHML_PARVE DHML_PARVE]] Methylamine dehydrogenase carries out the oxidation of methylamine. Electrons are passed from methylamine dehydrogenase to amicyanin. [[http://www.uniprot.org/uniprot/DHMH_PARVE DHMH_PARVE]] Methylamine dehydrogenase carries out the oxidation of methylamine. Electrons are passed from methylamine dehydrogenase to amicyanin. 
== 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/ma/1mae_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=1mae ConSurf].
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== Publication Abstract from PubMed ==
To identify the reactive part of the orthoquinone function of the tryptophan-derived cofactor found in methylamine dehydrogenase (MADH), we have determined the crystal structures of MADH from Thiobacillus versutus inhibited by methylhydrazine and (2,2,2-trifluoroethyl)hydrazine. Extra electron density attached to C6 of the tryptophyl tryptophanquinone cofactor shows that this atom and not C7 is the reactive part of the ortho-quinone moiety. The density retained after hydrazine inhibition is much less extensive than expected, however, suggesting that partial breakdown of the inhibitors after reaction with the cofactor may take place. A detailed description is presented of the cofactor environment in an improved model of MADH which now includes information from the recently determined gene sequence of the cofactor-containing subunit [Ubbink, M., van Kleef, M.A.G., Kleinjan, D., Hoitink, C.W.G., Huitema, F., Beintema, J.J., Duine, J.A., &amp; Canters, G.W. (1991) Eur. J. Biochem. 202, 1003-1012]. We hypothesize that Asp76 is responsible for proton abstraction from the alpha-carbon of the substrate during catalysis.

Active site structure of methylamine dehydrogenase: hydrazines identify C6 as the reactive site of the tryptophan-derived quinone cofactor.,Huizinga EG, van Zanten BA, Duine JA, Jongejan JA, Huitema F, Wilson KS, Hol WG Biochemistry. 1992 Oct 13;31(40):9789-95. PMID:1390754<ref>PMID:1390754</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1mae" style="background-color:#fffaf0;"></div>

==See Also==
*[[Methylamine dehydrogenase|Methylamine dehydrogenase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Atcc 25364]]
[[Category: Hol, W G.J]]
[[Category: Huizinga, E G]]
[[Category: Vellieux, F M.D]]