5o4n: Difference between revisions
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==Apo HcgC from Methanococcus maripaludis soaked with SAH and pyridinol== | ==Apo HcgC from Methanococcus maripaludis soaked with SAH and pyridinol== | ||
<StructureSection load='5o4n' size='340' side='right' caption='[[5o4n]], [[Resolution|resolution]] 2.05Å' scene=''> | <StructureSection load='5o4n' size='340' side='right'caption='[[5o4n]], [[Resolution|resolution]] 2.05Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5o4n]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5O4N OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[5o4n]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5O4N OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5O4N FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=9KH:6-carboxy+methyl-4-hydroxy-2-pyridinol'>9KH</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9KH:6-carboxy+methyl-4-hydroxy-2-pyridinol'>9KH</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</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'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5o4n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o4n OCA], [http://pdbe.org/5o4n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5o4n RCSB], [http://www.ebi.ac.uk/pdbsum/5o4n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5o4n ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</div> | </div> | ||
<div class="pdbe-citations 5o4n" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5o4n" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[SAM-dependent methyltrasferase 3D structures|SAM-dependent methyltrasferase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Bai, L]] | [[Category: Bai, L]] | ||
[[Category: Ermler, U]] | [[Category: Ermler, U]] | ||
Revision as of 15:17, 26 August 2020
Apo HcgC from Methanococcus maripaludis soaked with SAH and pyridinolApo HcgC from Methanococcus maripaludis soaked with SAH and pyridinol
Structural highlights
Publication Abstract from PubMed[Fe]-hydrogenase hosts an iron-guanylylpyridinol (FeGP) cofactor. The FeGP cofactor contains a pyridinol ring substituted with GMP, two methyl groups, and an acylmethyl group. HcgC, an enzyme involved in FeGP biosynthesis, catalyzes methyl transfer from S-adenosylmethionine (SAM) to C3 of 6-carboxymethyl-5-methyl-4-hydroxy-2-pyridinol (2). We report on the ternary structure of HcgC/S-adenosylhomocysteine (SAH, the demethylated product of SAM) and 2 at 1.7 A resolution. The proximity of C3 of substrate 2 and the S atom of SAH indicates a catalytically productive geometry. The hydroxy and carboxy groups of substrate 2 are hydrogen-bonded with I115 and T179, as well as through a series of water molecules linked with polar and a few protonatable groups. These interactions stabilize the deprotonated state of the hydroxy groups and a keto form of substrate 2, through which the nucleophilicity of C3 is increased by resonance effects. Complemented by mutational analysis, a structure-based catalytic mechanism was proposed. A Water-Bridged H-Bonding Network Contributes to the Catalysis of the SAM-Dependent C-Methyltransferase HcgC.,Bai L, Wagner T, Xu T, Hu X, Ermler U, Shima S Angew Chem Int Ed Engl. 2017 Jul 6. doi: 10.1002/anie.201705605. PMID:28682478[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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