7fbo: Difference between revisions
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==geranyl pyrophosphate C6-methyltransferase BezA binding with S-adenosylhomocysteine== | |||
<StructureSection load='7fbo' size='340' side='right'caption='[[7fbo]], [[Resolution|resolution]] 2.56Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7fbo]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._RI-18-2 Streptomyces sp. RI-18-2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7FBO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7FBO 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]] 2.56Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</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=7fbo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7fbo OCA], [https://pdbe.org/7fbo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7fbo RCSB], [https://www.ebi.ac.uk/pdbsum/7fbo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7fbo ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A2Z5X7B9_9ACTN A0A2Z5X7B9_9ACTN] [https://www.uniprot.org/uniprot/A0A1V4D079_9ACTN A0A1V4D079_9ACTN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Prenyl pyrophosphate methyltransferases enhance the structural diversity of terpenoids. However, the molecular basis of their catalytic mechanisms is poorly understood. In this study, using multiple strategies, we characterized a geranyl pyrophosphate (GPP) C6-methyltransferase, BezA. Biochemical analysis revealed that BezA requires Mg(2+) and solely methylates GPP. The crystal structures of BezA and its complex with S-adenosyl homocysteine were solved at 2.10 and 2.56 A, respectively. Further analyses using site-directed mutagenesis, molecular docking, molecular dynamics simulations, and quantum mechanics/molecular mechanics calculations revealed the molecular basis of the methylation reaction. Importantly, the function of E170 as a catalytic base to complete the methylation reaction was established. We also succeeded in switching the substrate specificity by introducing a W210A substitution, resulting in an unprecedented farnesyl pyrophosphate C6-methyltransferase. | |||
Structural and Molecular Basis of the Catalytic Mechanism of Geranyl Pyrophosphate C6-Methyltransferase: Creation of an Unprecedented Farnesyl Pyrophosphate C6-Methyltransferase.,Tsutsumi H, Moriwaki Y, Terada T, Shimizu K, Shin-Ya K, Katsuyama Y, Ohnishi Y Angew Chem Int Ed Engl. 2021 Oct 9. doi: 10.1002/anie.202111217. PMID:34626048<ref>PMID:34626048</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 7fbo" style="background-color:#fffaf0;"></div> | ||
[[Category: Katsuyama | == References == | ||
[[Category: | <references/> | ||
[[Category: Ohnishi | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Terada | [[Category: Large Structures]] | ||
[[Category: Streptomyces sp. RI-18-2]] | |||
[[Category: Katsuyama Y]] | |||
[[Category: Moriwaki Y]] | |||
[[Category: Ohnishi Y]] | |||
[[Category: Shimizu K]] | |||
[[Category: Terada T]] | |||
[[Category: Tsutsumi H]] | |||
Latest revision as of 17:12, 29 November 2023
geranyl pyrophosphate C6-methyltransferase BezA binding with S-adenosylhomocysteine
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