5d4u: Difference between revisions

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-'''Unreleased structure'''
-The entry 5d4u is ON HOLD  until Paper Publication
+==SAM-bound HcgC from Methanocaldococcus jannaschii==
+<StructureSection load='5d4u' size='340' side='right' caption='[[5d4u]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5d4u]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D4U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D4U FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5d4t|5d4t]]</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=5d4u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d4u OCA], [http://pdbe.org/5d4u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d4u RCSB], [http://www.ebi.ac.uk/pdbsum/5d4u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5d4u ProSAT]</span></td></tr>
+</table>
+<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.
-Authors: Fujishiro, T., Ermler, U., Shima, S.
+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>
-Description: SAM-bound HcgC from Methanocaldococcus jannaschii
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Shima, S]]
+<div class="pdbe-citations 5d4u" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Ermler, U]]
 [[Category: Fujishiro, T]]
+[[Category: Shima, S]]
+[[Category: Rossmann-like fold]]
+[[Category: Unknown function]]