4o1e: Difference between revisions

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==Structure of a methyltransferase component in complex with MTHF involved in O-demethylation==
==Structure of a methyltransferase component in complex with MTHF involved in O-demethylation==
<StructureSection load='4o1e' size='340' side='right' caption='[[4o1e]], [[Resolution|resolution]] 1.61&Aring;' scene=''>
<StructureSection load='4o1e' size='340' side='right'caption='[[4o1e]], [[Resolution|resolution]] 1.61&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4o1e]] 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=4O1E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O1E FirstGlance]. <br>
<table><tr><td colspan='2'>[[4o1e]] 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=4O1E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O1E FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=C2F:5-METHYL-5,6,7,8-TETRAHYDROFOLIC+ACID'>C2F</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.61&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4o0q|4o0q]], [[4o1f|4o1f]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C2F:5-METHYL-5,6,7,8-TETRAHYDROFOLIC+ACID'>C2F</scene></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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4o1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o1e OCA], [https://pdbe.org/4o1e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o1e RCSB], [https://www.ebi.ac.uk/pdbsum/4o1e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o1e ProSAT]</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=4o1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o1e OCA], [http://pdbe.org/4o1e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4o1e RCSB], [http://www.ebi.ac.uk/pdbsum/4o1e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4o1e ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/B8FW00_DESHD B8FW00_DESHD]
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>
==See Also==
 
*[[Dihydropteroate synthase 3D structures|Dihydropteroate synthase 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4o1e" style="background-color:#fffaf0;"></div>
== 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]]
[[Category: Transferase]]
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