1h4j

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[[Image:1h4j.gif|left|200px]]
 
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==Methylobacterium extorquens methanol dehydrogenase D303E mutant==
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The line below this paragraph, containing "STRUCTURE_1h4j", creates the "Structure Box" on the page.
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<StructureSection load='1h4j' size='340' side='right'caption='[[1h4j]], [[Resolution|resolution]] 3.00&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'>[[1h4j]] is a 8 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=1H4J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H4J 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]] 3&#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_1h4j| PDB=1h4j | 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=1h4j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h4j OCA], [https://pdbe.org/1h4j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h4j RCSB], [https://www.ebi.ac.uk/pdbsum/1h4j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h4j ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DHM1_METEA DHM1_METEA] 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/h4/1h4j_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=1h4j ConSurf].
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<div style="clear:both"></div>
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'''METHYLOBACTERIUM EXTORQUENS METHANOL DEHYDROGENASE D303E MUTANT'''
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==See Also==
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*[[Methanol dehydrogenase|Methanol dehydrogenase]]
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__TOC__
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==Overview==
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</StructureSection>
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Two proteins specifically involved in methanol oxidation in the methylotrophic bacterium Methylobacterium extorquens have been modified by site-directed mutagenesis. Mutation of the proposed active site base (Asp303) to glutamate in methanol dehydrogenase (MDH) gave an active enzyme (D303E-MDH) with a greatly reduced affinity for substrate and with a lower activation energy. Results of kinetic and deuterium isotope studies showed that the essential mechanism in the mutant protein was unchanged, and that the step requiring activation by ammonia remained rate limiting. No spectrally detectable intermediates could be observed during the reaction. The X-ray structure, determined to 3 A resolution, of D303E-MDH showed that the position and coordination geometry of the Ca2+ ion in the active site was altered; the larger Glu303 side chain was coordinated to the Ca2+ ion and also hydrogen bonded to the O5 atom of pyrroloquinoline quinone (PQQ). The properties and structure of the D303E-MDH are consistent with the previous proposal that the reaction in MDH is initiated by proton abstraction involving Asp303, and that the mechanism involves a direct hydride transfer reaction. Mutation of the two adjacent cysteine residues that make up the novel disulfide ring in the active site of MDH led to an inactive enzyme, confirming the essential role of this remarkable ring structure. Mutations of cytochrome c(L), which is the electron acceptor from MDH was used to identify Met109 as the sixth ligand to the heme.
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[[Category: Large Structures]]
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[[Category: Methylorubrum extorquens]]
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==About this Structure==
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[[Category: Afolabi PR]]
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1H4J is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Methylobacterium_extorquens Methylobacterium extorquens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H4J OCA].
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[[Category: Anthony C]]
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[[Category: Cooper JB]]
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==Reference==
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[[Category: Gill R]]
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Site-directed mutagenesis and X-ray crystallography of the PQQ-containing quinoprotein methanol dehydrogenase and its electron acceptor, cytochrome c(L)., Afolabi PR, Mohammed F, Amaratunga K, Majekodunmi O, Dales SL, Gill R, Thompson D, Cooper JB, Wood SP, Goodwin PM, Anthony C, Biochemistry. 2001 Aug 21;40(33):9799-809. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11502173 11502173]
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[[Category: Mohammed F]]
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[[Category: Methylobacterium extorquens]]
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[[Category: Thompson D]]
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[[Category: Protein complex]]
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[[Category: Wood SP]]
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[[Category: Afolabi, P R.]]
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[[Category: Anthony, C.]]
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[[Category: Cooper, J B.]]
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[[Category: Gill, R.]]
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[[Category: Mohammed, F.]]
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[[Category: Thompson, D.]]
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[[Category: Wood, S P.]]
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[[Category: Dehydrogenase]]
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[[Category: Quinoprotein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:25:18 2008''
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Current revision

Methylobacterium extorquens methanol dehydrogenase D303E mutant

PDB ID 1h4j

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