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| | ==Apo structure of a methyltransferase component involved in O-demethylation== | | ==Apo structure of a methyltransferase component involved in O-demethylation== |
| - | <StructureSection load='4o0q' size='340' side='right' caption='[[4o0q]], [[Resolution|resolution]] 1.92Å' scene=''> | + | <StructureSection load='4o0q' size='340' side='right'caption='[[4o0q]], [[Resolution|resolution]] 1.92Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4o0q]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Deshd Deshd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O0Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O0Q FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4o0q]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Desulfitobacterium_hafniense_DCB-2 Desulfitobacterium hafniense DCB-2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O0Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O0Q FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4o1f|4o1f]], [[4o1e|4o1e]]</td></tr> | + | </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=4o0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o0q OCA], [https://pdbe.org/4o0q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o0q RCSB], [https://www.ebi.ac.uk/pdbsum/4o0q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o0q ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Dhaf_0722 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272564 DESHD])</td></tr>
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| - | <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=4o0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o0q OCA], [http://pdbe.org/4o0q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4o0q RCSB], [http://www.ebi.ac.uk/pdbsum/4o0q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4o0q ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/B8FW00_DESHD B8FW00_DESHD] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4o0q" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4o0q" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Dihydropteroate synthase 3D structures|Dihydropteroate synthase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Deshd]] | + | [[Category: Desulfitobacterium hafniense DCB-2]] |
| - | [[Category: Dunstan, M S]] | + | [[Category: Large Structures]] |
| - | [[Category: Fisher, K]] | + | [[Category: Dunstan MS]] |
| - | [[Category: Leys, D]] | + | [[Category: Fisher K]] |
| - | [[Category: Sjuts, H]] | + | [[Category: Leys D]] |
| - | [[Category: Methyltransferase]]
| + | [[Category: Sjuts H]] |
| - | [[Category: Thf/mthf]]
| + | |
| - | [[Category: Tim barrel]]
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| - | [[Category: Transferase]]
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| Structural highlights
Function
B8FW00_DESHD
Publication Abstract from PubMed
O-Demethylation by acetogenic or organohalide-respiring bacteria leads to the formation of methyltetrahydrofolate from aromatic methyl ethers. O-Demethylases, which are cobalamin-dependent, three-component enzyme systems, catalyse methyl-group transfers from aromatic methyl ethers to tetrahydrofolate via methylcobalamin intermediates. In this study, crystal structures of the tetrahydrofolate-binding methyltransferase module from a Desulfitobacterium hafniense DCB-2 O-demethylase were determined both in complex with tetrahydrofolate and the product methyltetrahydrofolate. While these structures are similar to previously determined methyltransferase structures, the position of key active-site residues is subtly altered. A strictly conserved Asn is displaced to establish a putative proton-transfer network between the substrate N5 and solvent. It is proposed that this supports the efficient catalysis of methyltetrahydrofolate formation, which is necessary for efficient O-demethylation.
Structures of the methyltransferase component of Desulfitobacterium hafniense DCB-2 O-demethylase shed light on methyltetrahydrofolate formation.,Sjuts H, Dunstan MS, Fisher K, Leys D Acta Crystallogr D Biol Crystallogr. 2015 Sep 1;71(Pt 9):1900-8. doi:, 10.1107/S1399004715013061. Epub 2015 Aug 25. PMID:26327380[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sjuts H, Dunstan MS, Fisher K, Leys D. Structures of the methyltransferase component of Desulfitobacterium hafniense DCB-2 O-demethylase shed light on methyltetrahydrofolate formation. Acta Crystallogr D Biol Crystallogr. 2015 Sep 1;71(Pt 9):1900-8. doi:, 10.1107/S1399004715013061. Epub 2015 Aug 25. PMID:26327380 doi:http://dx.doi.org/10.1107/S1399004715013061
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