1h4j

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<StructureSection load='1h4j' size='340' side='right'caption='[[1h4j]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
<StructureSection load='1h4j' size='340' side='right'caption='[[1h4j]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1h4j]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_extorquens"_bassalik_1913 "bacillus extorquens" bassalik 1913]. 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 [http://proteopedia.org/fgij/fg.htm?mol=1H4J FirstGlance]. <br>
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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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</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>
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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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1h4i|1h4i]]</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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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">moxF, mxaF, MexAM1_META1p4538 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=408 "Bacillus extorquens" Bassalik 1913]), moxI, mxaI, MexAM1_META1p4535 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=408 "Bacillus extorquens" Bassalik 1913])</td></tr>
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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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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methanol_dehydrogenase_(cytochrome_c) Methanol dehydrogenase (cytochrome c)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.2.7 1.1.2.7] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1h4j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h4j OCA], [http://pdbe.org/1h4j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1h4j RCSB], [http://www.ebi.ac.uk/pdbsum/1h4j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1h4j ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/DHM1_METEA DHM1_METEA]] Catalyzes the oxidation of primary alcohols including methanol. [[http://www.uniprot.org/uniprot/DHM2_METEA DHM2_METEA]] Catalyzes the oxidation of primary alcohols including methanol.
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[https://www.uniprot.org/uniprot/DHM1_METEA DHM1_METEA] Catalyzes the oxidation of primary alcohols including methanol.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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].
</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].
<div style="clear:both"></div>
<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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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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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:11502173<ref>PMID:11502173</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 1h4j" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Methanol dehydrogenase|Methanol dehydrogenase]]
*[[Methanol dehydrogenase|Methanol dehydrogenase]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacillus extorquens bassalik 1913]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Afolabi, P R]]
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[[Category: Methylorubrum extorquens]]
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[[Category: Anthony, C]]
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[[Category: Afolabi PR]]
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[[Category: Cooper, J B]]
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[[Category: Anthony C]]
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[[Category: Gill, R]]
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[[Category: Cooper JB]]
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[[Category: Mohammed, F]]
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[[Category: Gill R]]
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[[Category: Thompson, D]]
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[[Category: Mohammed F]]
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[[Category: Wood, S P]]
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[[Category: Thompson D]]
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[[Category: Dehydrogenase]]
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[[Category: Wood SP]]
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[[Category: Oxidoreductase]]
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[[Category: Quinoprotein]]
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Current revision

Methylobacterium extorquens methanol dehydrogenase D303E mutant

PDB ID 1h4j

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