5d5o
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==HcgC from Methanocaldococcus jannaschii== | |
| + | <StructureSection load='5d5o' size='340' side='right'caption='[[5d5o]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5d5o]] 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=5D5O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5D5O 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]] 2.7Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5d5o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d5o OCA], [https://pdbe.org/5d5o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5d5o RCSB], [https://www.ebi.ac.uk/pdbsum/5d5o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5d5o 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 5d5o" 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]] | ||
Current revision
HcgC from Methanocaldococcus jannaschii
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