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1g72

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[[Image:1g72.png|left|200px]]
 
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==CATALYTIC MECHANISM OF QUINOPROTEIN METHANOL DEHYDROGENASE: A THEORETICAL AND X-RAY CRYSTALLOGRAPHIC INVESTIGATION==
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The line below this paragraph, containing "STRUCTURE_1g72", creates the "Structure Box" on the page.
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<StructureSection load='1g72' size='340' side='right'caption='[[1g72]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1g72]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylophilus_methylotrophus_W3A1 Methylophilus methylotrophus W3A1]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1G72 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PQQ:PYRROLOQUINOLINE+QUINONE'>PQQ</scene></td></tr>
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{{STRUCTURE_1g72| PDB=1g72 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1g72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g72 OCA], [https://pdbe.org/1g72 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g72 RCSB], [https://www.ebi.ac.uk/pdbsum/1g72 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g72 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DHM1_METME DHM1_METME] Catalyzes the oxidation of primary alcohols including methanol.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g7/1g72_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1g72 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===CATALYTIC MECHANISM OF QUINOPROTEIN METHANOL DEHYDROGENASE: A THEORETICAL AND X-RAY CRYSTALLOGRAPHIC INVESTIGATION===
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1g72" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_11149955}}, adds the Publication Abstract to the page
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*[[Methanol dehydrogenase|Methanol dehydrogenase]]
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(as it appears on PubMed at http://www.pubmed.gov), where 11149955 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_11149955}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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[[1g72]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Methylophilus_methylotrophus_w3a1 Methylophilus methylotrophus w3a1]. 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].
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[[Category: Methylophilus methylotrophus W3A1]]
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[[Category: Bruice TC]]
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==Reference==
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[[Category: Chen Z]]
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<ref group="xtra">PMID:11149955</ref><references group="xtra"/>
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[[Category: Mathews FS]]
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[[Category: Methylophilus methylotrophus w3a1]]
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[[Category: Xia Z]]
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[[Category: Bruice, T C.]]
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[[Category: Zheng Y]]
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[[Category: Chen, Z.]]
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[[Category: Mathews, F S.]]
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[[Category: Xia, Z.]]
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[[Category: Zheng, Y.]]
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[[Category: Oxidoreductase]]
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[[Category: Quinoprotein]]
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Current revision

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

PDB ID 1g72

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