4o1f: Difference between revisions
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==Structure of a methyltransferase component in complex with THF involved in O-demethylation== | |||
<StructureSection load='4o1f' size='340' side='right'caption='[[4o1f]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4o1f]] 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=4O1F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O1F FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=THG:(6S)-5,6,7,8-TETRAHYDROFOLATE'>THG</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=4o1f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o1f OCA], [https://pdbe.org/4o1f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o1f RCSB], [https://www.ebi.ac.uk/pdbsum/4o1f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o1f ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/B8FW00_DESHD B8FW00_DESHD] | |||
<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 4o1f" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Dihydropteroate synthase 3D structures|Dihydropteroate synthase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Desulfitobacterium hafniense DCB-2]] | |||
[[Category: Large Structures]] | |||
[[Category: Dunstan MS]] | |||
[[Category: Fisher K]] | |||
[[Category: Leys D]] | |||
[[Category: Sjuts H]] | |||
Latest revision as of 17:52, 8 November 2023
Structure of a methyltransferase component in complex with THF involved in O-demethylationStructure of a methyltransferase component in complex with THF involved in O-demethylation
Structural highlights
FunctionPublication Abstract from PubMedO-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 AlsoReferences
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