2ad7: Difference between revisions
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== | ==crystal structure of methanol dehydrogenase from M. W3A1 (form C) in the presence of methanol== | ||
<StructureSection load='2ad7' size='340' side='right'caption='[[2ad7]], [[Resolution|resolution]] 1.50Å' scene=''> | |||
== Structural highlights == | |||
[ | <table><tr><td colspan='2'>[[2ad7]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylophilus_methylotrophus_W3A1 Methylophilus methylotrophus W3A1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AD7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AD7 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]] 1.5Å</td></tr> | |||
[ | <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> | ||
[[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ad7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ad7 OCA], [https://pdbe.org/2ad7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ad7 RCSB], [https://www.ebi.ac.uk/pdbsum/2ad7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ad7 ProSAT]</span></td></tr> | ||
</table> | |||
[ | == Function == | ||
[[ | [https://www.uniprot.org/uniprot/DHM2_METME DHM2_METME] Catalyzes the oxidation of primary alcohols including methanol (By similarity). | ||
[ | == 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/2ad7_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=2ad7 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Methanol dehydrogenase is a heterotetrameric enzyme containing the prosthetic group pyrroloquinoline quinone (PQQ), which catalyzes the oxidation of methanol to formaldehyde. The crystal structure of methanol dehydrogenase from Methylophilus W3A1, previously determined at high resolution, exhibits a non-planar configuration of the PQQ ring system and lends support for a hydride transfer mechanism of the enzymatic reaction catalyzed by the enzyme. To investigate why PQQ is in the C5-reduced form and to better understand the catalytic mechanism of the enzyme, three structures of this enzyme in a new crystal form have been determined at higher resolution. Two of the three crystals were grown in the presence of 1 and 50 mM methanol, respectively, both structures of which show non-planar configurations of the PQQ ring system, confirming the previous conclusion; the other was crystallized in the presence of 50 mM ethanol, the structure of which displays a planar ring system for PQQ. Comparison of these structures reveals that the configuration change of PQQ is induced by the enzymatic reaction. The reaction takes place and the C5-reduced PQQ intermediate is produced when the enzyme co-crystallizes with methanol, but the enzymatic reaction does not take place and the PQQ ring retains a planar configuration of the oxidized orthoquinone form when ethanol instead of methanol is present in the crystallization solution. | |||
The enzymatic reaction-induced configuration change of the prosthetic group PQQ of methanol dehydrogenase.,Li J, Gan JH, Mathews FS, Xia ZX Biochem Biophys Res Commun. 2011 Mar 25;406(4):621-6. Epub 2011 Feb 26. PMID:21356200<ref>PMID:21356200</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2ad7" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Methanol dehydrogenase|Methanol dehydrogenase]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Methylophilus methylotrophus W3A1]] | |||
[[Category: Gan J-H]] | |||
[[Category: Li J]] | |||
[[Category: Mathews FS]] | |||
[[Category: Xia Z-X]] | |||
Latest revision as of 11:59, 6 November 2024
crystal structure of methanol dehydrogenase from M. W3A1 (form C) in the presence of methanolcrystal structure of methanol dehydrogenase from M. W3A1 (form C) in the presence of methanol
Structural highlights
FunctionDHM2_METME Catalyzes the oxidation of primary alcohols including methanol (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedMethanol dehydrogenase is a heterotetrameric enzyme containing the prosthetic group pyrroloquinoline quinone (PQQ), which catalyzes the oxidation of methanol to formaldehyde. The crystal structure of methanol dehydrogenase from Methylophilus W3A1, previously determined at high resolution, exhibits a non-planar configuration of the PQQ ring system and lends support for a hydride transfer mechanism of the enzymatic reaction catalyzed by the enzyme. To investigate why PQQ is in the C5-reduced form and to better understand the catalytic mechanism of the enzyme, three structures of this enzyme in a new crystal form have been determined at higher resolution. Two of the three crystals were grown in the presence of 1 and 50 mM methanol, respectively, both structures of which show non-planar configurations of the PQQ ring system, confirming the previous conclusion; the other was crystallized in the presence of 50 mM ethanol, the structure of which displays a planar ring system for PQQ. Comparison of these structures reveals that the configuration change of PQQ is induced by the enzymatic reaction. The reaction takes place and the C5-reduced PQQ intermediate is produced when the enzyme co-crystallizes with methanol, but the enzymatic reaction does not take place and the PQQ ring retains a planar configuration of the oxidized orthoquinone form when ethanol instead of methanol is present in the crystallization solution. The enzymatic reaction-induced configuration change of the prosthetic group PQQ of methanol dehydrogenase.,Li J, Gan JH, Mathews FS, Xia ZX Biochem Biophys Res Commun. 2011 Mar 25;406(4):621-6. Epub 2011 Feb 26. PMID:21356200[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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