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1h4i
From Proteopedia
(Difference between revisions)
(New page: 200px<br /> <applet load="1h4i" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h4i, resolution 1.94Å" /> '''METHYLOBACTERIUM EX...) |
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| - | [[Image:1h4i.gif|left|200px]]<br /> | ||
| - | <applet load="1h4i" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1h4i, resolution 1.94Å" /> | ||
| - | '''METHYLOBACTERIUM EXTORQUENS METHANOL DEHYDROGENASE'''<br /> | ||
| - | == | + | ==Methylobacterium extorquens methanol dehydrogenase== |
| - | BACKGROUND: Methanol dehydrogenase (MDH) is a bacterial periplasmic | + | <StructureSection load='1h4i' size='340' side='right'caption='[[1h4i]], [[Resolution|resolution]] 1.94Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1h4i]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylorubrum_extorquens Methylorubrum extorquens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H4I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H4I 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]] 1.94Å</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=1h4i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h4i OCA], [https://pdbe.org/1h4i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h4i RCSB], [https://www.ebi.ac.uk/pdbsum/1h4i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h4i ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/DHM1_METEA DHM1_METEA] Catalyzes the oxidation of primary alcohols including methanol. | ||
| + | == 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/h4/1h4i_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=1h4i ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | BACKGROUND: Methanol dehydrogenase (MDH) is a bacterial periplasmic quinoprotein; it has pyrrolo-quinoline quinone (PQQ) as its prosthetic group, requires Ca2+ for activity and uses cytochrome cL as its electron acceptor. Low-resolution structures of MDH have already been determined. RESULTS: The structure of the alpha 2 beta 2 tetramer of MDH from Methylobacterium extorquens has now been determined at 1.94 A with an R-factor of 19.85%. CONCLUSIONS: The alpha-subunit of MDH has an eight-fold radial symmetry, with its eight beta-sheets stabilized by a novel tryptophan docking motif. The PQQ in the active site is held in place by a coplanar tryptophan and by a novel disulphide ring formed between adjacent cysteines which are bonded by an unusual non-planar trans peptide bond. One of the carbonyl oxygens of PQQ is bonded to the Ca2+, probably facilitating attack on the substrate, and the other carbonyl oxygen is out of the plane of the ring, confirming the presence of the predicted free-radical semiquinone form of the prosthetic group. | ||
| - | + | The refined structure of the quinoprotein methanol dehydrogenase from Methylobacterium extorquens at 1.94 A.,Ghosh M, Anthony C, Harlos K, Goodwin MG, Blake C Structure. 1995 Feb 15;3(2):177-87. PMID:7735834<ref>PMID:7735834</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1h4i" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Methanol dehydrogenase|Methanol dehydrogenase]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Methylorubrum extorquens]] | ||
| + | [[Category: Anthony C]] | ||
| + | [[Category: Blake C]] | ||
| + | [[Category: Ghosh M]] | ||
| + | [[Category: Goodwin MG]] | ||
| + | [[Category: Harlos K]] | ||
Current revision
Methylobacterium extorquens methanol dehydrogenase
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