8gy2: Difference between revisions

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-'''Unreleased structure'''
-The entry 8gy2 is ON HOLD
+==Cryo-EM Structure of Membrane-Bound Alcohol Dehydrogenase from Gluconobacter oxydans==
+<StructureSection load='8gy2' size='340' side='right'caption='[[8gy2]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
-Authors:
+== Structural highlights ==
+<table><tr><td colspan='2'>[[8gy2]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Gluconobacter_oxydans Gluconobacter oxydans] and [https://en.wikipedia.org/wiki/Gluconobacter_oxydans_621H Gluconobacter oxydans 621H]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8GY2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8GY2 FirstGlance]. <br>
-Description:
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
-[[Category: Unreleased Structures]]
+<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=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=PQQ:PYRROLOQUINOLINE+QUINONE'>PQQ</scene>, <scene name='pdbligand=U10:UBIQUINONE-10'>U10</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=8gy2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8gy2 OCA], [https://pdbe.org/8gy2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8gy2 RCSB], [https://www.ebi.ac.uk/pdbsum/8gy2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8gy2 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/ADHA_GLUOX ADHA_GLUOX] Dehydrogenase component of the alcohol dehydrogenase multicomponent enzyme system which is involved in the production of acetic acid and in the ethanol oxidase respiratory chain. Quinohemoprotein alcohol dehydrogenase (ADH) catalyzes the oxidation of ethanol to acetaldehyde by transferring electrons to the ubiquinone embedded in the membrane phospholipids (PubMed:1646200, PubMed:7592433, PubMed:8617755, PubMed:9878716, PubMed:18838797). The electrons transfer from ethanol to membranous ubiquinone occurs from pyrroloquinoline quinone (PQQ) to one heme c in subunit I (AdhA), and finally to two heme c in subunit II (AdhB) (PubMed:8617755, PubMed:9878716, PubMed:18838797). Besides ubiquinone reduction, ADH also has a ubiquinol (QH2) oxidation reaction which mediates electron transfer from ubiquinol to the non-energy generating bypass oxidase system (PubMed:9878716). The electrons transfer occurs from ubiquinol (QH2) to the additional heme c within subunit II (AdhB) (PubMed:8617755, PubMed:9878716). Also able to use quinone analogs such as 2,3-dimethoxy-5-methyl-6-n-decyl-1,4-benzoquinone (DB) and 2,3-dimethoxy-5-methyl-6-n-pentyl-1,4-benzoquinone (PB) (PubMed:9878716).<ref>PMID:1646200</ref> <ref>PMID:18838797</ref> <ref>PMID:7592433</ref> <ref>PMID:8617755</ref> <ref>PMID:9878716</ref> <ref>PMID:9055427</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Gluconobacter oxydans]]
+[[Category: Gluconobacter oxydans 621H]]
+[[Category: Large Structures]]
+[[Category: Adachi T]]
+[[Category: Kitazumi Y]]
+[[Category: Makino F]]
+[[Category: Miyata T]]
+[[Category: Namba K]]
+[[Category: Shirai O]]
+[[Category: Sowa K]]
+[[Category: Tanaka H]]