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| | <StructureSection load='4obx' size='340' side='right'caption='[[4obx]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='4obx' size='340' side='right'caption='[[4obx]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4obx]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OBX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OBX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4obx]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OBX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OBX FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TAM:TRIS(HYDROXYETHYL)AMINOMETHANE'>TAM</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TAM:TRIS(HYDROXYETHYL)AMINOMETHANE'>TAM</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4obw|4obw]]</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=4obx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4obx OCA], [https://pdbe.org/4obx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4obx RCSB], [https://www.ebi.ac.uk/pdbsum/4obx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4obx ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">COQ5, DBI56, YM8339.09C, YML110C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/2-methoxy-6-polyprenyl-1,4-benzoquinol_methylase 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.201 2.1.1.201] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4obx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4obx OCA], [http://pdbe.org/4obx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4obx RCSB], [http://www.ebi.ac.uk/pdbsum/4obx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4obx ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/COQ5_YEAST COQ5_YEAST]] Methyltransferase required for the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2). | + | [https://www.uniprot.org/uniprot/COQ5_YEAST COQ5_YEAST] Methyltransferase required for the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase]] | |
| - | [[Category: Baker's yeast]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Cao, D D]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Chen, Y X]] | + | [[Category: Cao DD]] |
| - | [[Category: Chi, C B]] | + | [[Category: Chen YX]] |
| - | [[Category: Dai, Y N]] | + | [[Category: Chi CB]] |
| - | [[Category: Jiang, Y L]] | + | [[Category: Dai YN]] |
| - | [[Category: Meng, F]] | + | [[Category: Jiang YL]] |
| - | [[Category: Ren, Y M]] | + | [[Category: Meng F]] |
| - | [[Category: Zhou, C Z]] | + | [[Category: Ren YM]] |
| - | [[Category: Zhou, K]] | + | [[Category: Zhou CZ]] |
| - | [[Category: Methyltransferase]]
| + | [[Category: Zhou K]] |
| - | [[Category: Rossmann fold]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
COQ5_YEAST Methyltransferase required for the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2).
Publication Abstract from PubMed
Saccharomyces cerevisiae Coq5 is an S-adenosyl methionine (SAM)-dependent methyltransferase (SAM-MTase) that catalyzes the only C-methylation step in the coenzyme Q (CoQ) biosynthesis pathway, in which 2-methoxy-6-polyprenyl-1,4-benzoquinone (DDMQH2) is converted to 2-methoxy-5-methyl-6-polyprenyl-1,4-benzoquinone (DMQH2). Crystal structures of Coq5 were determined in the apo form (Coq5-apo) at 2.2 A resolution and in the SAM-bound form (Coq5-SAM) at 2.4 A resolution, representing the first pair of structures for the yeast CoQ biosynthetic enzymes. Coq5 displays a typical class I SAM-MTase structure with two minor variations beyond the core domain, both of which are considered to participate in dimerization and/or substrate recognition. Slight conformational changes at the active-site pocket were observed upon binding of SAM. Structure-based computational simulation using an analogue of DDMQH2 enabled us to identify the binding pocket and entrance tunnel of the substrate. Multiple-sequence alignment showed that the residues contributing to the dimeric interface and the SAM- and DDMQH2-binding sites are highly conserved in Coq5 and homologues from diverse species. A putative catalytic mechanism of Coq5 was proposed in which Arg201 acts as a general base to initiate catalysis with the help of a water molecule.
Crystal structures and catalytic mechanism of the C-methyltransferase Coq5 provide insights into a key step of the yeast coenzyme Q synthesis pathway.,Dai YN, Zhou K, Cao DD, Jiang YL, Meng F, Chi CB, Ren YM, Chen Y, Zhou CZ Acta Crystallogr D Biol Crystallogr. 2014 Aug 1;70(Pt 8):2085-92. doi:, 10.1107/S1399004714011559. Epub 2014 Jul 25. PMID:25084328[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Dai YN, Zhou K, Cao DD, Jiang YL, Meng F, Chi CB, Ren YM, Chen Y, Zhou CZ. Crystal structures and catalytic mechanism of the C-methyltransferase Coq5 provide insights into a key step of the yeast coenzyme Q synthesis pathway. Acta Crystallogr D Biol Crystallogr. 2014 Aug 1;70(Pt 8):2085-92. doi:, 10.1107/S1399004714011559. Epub 2014 Jul 25. PMID:25084328 doi:http://dx.doi.org/10.1107/S1399004714011559
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