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{{STRUCTURE_1g72|  PDB=1g72  |  SCENE=  }}
==CATALYTIC MECHANISM OF QUINOPROTEIN METHANOL DEHYDROGENASE: A THEORETICAL AND X-RAY CRYSTALLOGRAPHIC INVESTIGATION==
===CATALYTIC MECHANISM OF QUINOPROTEIN METHANOL DEHYDROGENASE: A THEORETICAL AND X-RAY CRYSTALLOGRAPHIC INVESTIGATION===
<StructureSection load='1g72' size='340' side='right' caption='[[1g72]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
{{ABSTRACT_PUBMED_11149955}}
== Structural highlights ==
<table><tr><td colspan='2'>[[1g72]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Methylophilus_methylotrophus Methylophilus methylotrophus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1b2n 1b2n]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G72 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G72 FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PQQ:PYRROLOQUINOLINE+QUINONE'>PQQ</scene><br>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4aah|4aah]]</td></tr>
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alcohol_dehydrogenase_(acceptor) Alcohol dehydrogenase (acceptor)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.99.8 1.1.99.8] </span></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g72 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1g72 RCSB], [http://www.ebi.ac.uk/pdbsum/1g72 PDBsum]</span></td></tr>
<table>
== 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/g7/1g72_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/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The catalytic mechanism of the reductive half reaction of the quinoprotein methanol dehydrogenase (MDH) is believed to proceed either through a hemiketal intermediate or by direct transfer of a hydride ion from the substrate methyl group to the cofactor, pyrroloquinoline quinone (PQQ). A crystal structure of the enzyme-substrate complex of a similar quinoprotein, glucose dehydrogenase, has recently been reported that strongly favors the hydride transfer mechanism in that enzyme. A theoretical analysis and an improved refinement of the 1.9-A resolution crystal structure of MDH from Methylophilus methylotrophus W3A1 in the presence of methanol, reported earlier, indicates that the observed tetrahedral configuration of the C-5 atom of PQQ in that study represents the C-5-reduced form of the cofactor and lends support for a hydride transfer mechanism for MDH.


==Function==
Catalytic mechanism of quinoprotein methanol dehydrogenase: A theoretical and x-ray crystallographic investigation.,Zheng YJ, Xia Zx, Chen Zw, Mathews FS, Bruice TC Proc Natl Acad Sci U S A. 2001 Jan 16;98(2):432-4. Epub 2001 Jan 9. PMID:11149955<ref>PMID:11149955</ref>
[[http://www.uniprot.org/uniprot/DHM1_METME DHM1_METME]] Catalyzes the oxidation of primary alcohols including methanol. [[http://www.uniprot.org/uniprot/DHM2_METME DHM2_METME]] Catalyzes the oxidation of primary alcohols including methanol (By similarity).  


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[1g72]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Methylophilus_methylotrophus Methylophilus methylotrophus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1b2n 1b2n]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G72 OCA].
</div>


==See Also==
==See Also==
*[[Methanol dehydrogenase|Methanol dehydrogenase]]
*[[Methanol dehydrogenase|Methanol dehydrogenase]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:011149955</ref><references group="xtra"/><references/>
__TOC__
</StructureSection>
[[Category: Methylophilus methylotrophus]]
[[Category: Methylophilus methylotrophus]]
[[Category: Bruice, T C.]]
[[Category: Bruice, T C.]]

Revision as of 04:11, 3 October 2014

CATALYTIC MECHANISM OF QUINOPROTEIN METHANOL DEHYDROGENASE: A THEORETICAL AND X-RAY CRYSTALLOGRAPHIC INVESTIGATION

1g72, resolution 1.90Å

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