1h4i

<table><tr><td colspan='2'>[[1h4i]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylobacterium_extorquens Methylobacterium 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='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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1h4j|1h4j]]</div></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.2.7 and 1.1.2.8 1.1.2.7 and 1.1.2.8] </span></td></tr>

[[https://www.uniprot.org/uniprot/DHM1_METEA DHM1_METEA]] Catalyzes the oxidation of primary alcohols including methanol. [[https://www.uniprot.org/uniprot/DHM2_METEA DHM2_METEA]] Catalyzes the oxidation of primary alcohols including methanol.

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== 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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Methylobacterium extorquens]]

[[Category: Oxidoreductase]]

[[Category: Anthony, C]]

[[Category: Blake, C]]

[[Category: Ghosh, M]]

[[Category: Goodwin, M G]]

[[Category: Harlos, K]]

[[Category: Quinoprotein]]