5d4t: Difference between revisions
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New page: '''Unreleased structure''' The entry 5d4t is ON HOLD until Paper Publication Authors: Fujishiro, T., Ermler, U., Shima, S. Description: SeMet-labelled HcgC from Methanocaldococcus jann... |
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==SeMet-labelled HcgC from Methanocaldococcus jannaschii in space group P212121== | |||
<StructureSection load='5d4t' size='340' side='right'caption='[[5d4t]], [[Resolution|resolution]] 2.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5d4t]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D4T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5D4T FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=5d4t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d4t OCA], [https://pdbe.org/5d4t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5d4t RCSB], [https://www.ebi.ac.uk/pdbsum/5d4t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5d4t ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Y489_METJA Y489_METJA] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Previous retrosynthetic and isotope-labeling studies have indicated that biosynthesis of the iron guanylylpyridinol (FeGP) cofactor of [Fe]-hydrogenase requires a methyltransferase. This hypothetical enzyme covalently attaches the methyl group at the 3-position of the pyridinol ring. We describe the identification of HcgC, a gene product of the hcgA-G cluster responsible for FeGP cofactor biosynthesis. It acts as an S-adenosylmethionine (SAM)-dependent methyltransferase, based on the crystal structures of HcgC and the HcgC/SAM and HcgC/S-adenosylhomocysteine (SAH) complexes. The pyridinol substrate, 6-carboxymethyl-5-methyl-4-hydroxy-2-pyridinol, was predicted based on properties of the conserved binding pocket and substrate docking simulations. For verification, the assumed substrate was synthesized and used in a kinetic assay. Mass spectrometry and NMR analysis revealed 6-carboxymethyl-3,5-dimethyl-4-hydroxy-2-pyridinol as the reaction product, which confirmed the function of HcgC. | |||
Identification of HcgC as a SAM-Dependent Pyridinol Methyltransferase in [Fe]-Hydrogenase Cofactor Biosynthesis.,Fujishiro T, Bai L, Xu T, Xie X, Schick M, Kahnt J, Rother M, Hu X, Ermler U, Shima S Angew Chem Int Ed Engl. 2016 Jul 8. doi: 10.1002/anie.201604352. PMID:27391308<ref>PMID:27391308</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5d4t" style="background-color:#fffaf0;"></div> | ||
[[Category: Ermler | == References == | ||
[[Category: Fujishiro | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Methanocaldococcus jannaschii]] | |||
[[Category: Ermler U]] | |||
[[Category: Fujishiro T]] | |||
[[Category: Shima S]] | |||
Latest revision as of 10:22, 21 June 2023
SeMet-labelled HcgC from Methanocaldococcus jannaschii in space group P212121
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