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4o0q
From Proteopedia
(Difference between revisions)
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<table><tr><td colspan='2'>[[4o0q]] is a 2 chain structure. 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. 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> | ||
</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4o1f|4o1f]], [[4o1e|4o1e]]</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=4o0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o0q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o0q RCSB], [http://www.ebi.ac.uk/pdbsum/4o0q PDBsum]</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=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]</span></td></tr> |
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:26327380</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4o0q" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Dihydropteroate synthase|Dihydropteroate synthase]] | *[[Dihydropteroate synthase|Dihydropteroate synthase]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 06:00, 30 September 2015
Apo structure of a methyltransferase component involved in O-demethylation
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Categories: Dunstan, M S | Fisher, K | Leys, D | Sjuts, H | Methyltransferase | Thf/mthf | Tim barrel | Transferase
