3wv8
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==ATP-bound HcgE from Methanothermobacter marburgensis== |
| + | <StructureSection load='3wv8' size='340' side='right' caption='[[3wv8]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3wv8]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WV8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WV8 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</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">[[3wv7|3wv7]], [[3wv9|3wv9]], [[3wva|3wva]], [[3wvb|3wvb]], [[3wvc|3wvc]]</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=3wv8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wv8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wv8 RCSB], [http://www.ebi.ac.uk/pdbsum/3wv8 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The iron-guanylylpyridinol (FeGP) cofactor of [Fe]-hydrogenase contains a prominent iron centre with an acyl-Fe bond and is the only acyl-organometallic iron compound found in nature. Here, we identify the functions of HcgE and HcgF, involved in the biosynthesis of the FeGP cofactor using structure-to-function strategy. Analysis of the HcgE and HcgF crystal structures with and without bound substrates suggest that HcgE catalyses the adenylylation of the carboxy group of guanylylpyridinol (GP) to afford AMP-GP, and subsequently HcgF catalyses the transesterification of AMP-GP to afford a Cys (HcgF)-S-GP thioester. Both enzymatic reactions are confirmed by in vitro assays. The structural data also offer plausible catalytic mechanisms. This strategy of thioester activation corresponds to that used for ubiquitin activation, a key event in the regulation of multiple cellular processes. It further implicates a nucleophilic attack onto the acyl carbon presumably via an electron-rich Fe(0)- or Fe(I)-carbonyl complex in the Fe-acyl formation. | ||
| - | + | Protein-pyridinol thioester precursor for biosynthesis of the organometallic acyl-iron ligand in [Fe]-hydrogenase cofactor.,Fujishiro T, Kahnt J, Ermler U, Shima S Nat Commun. 2015 Apr 17;6:6895. doi: 10.1038/ncomms7895. PMID:25882909<ref>PMID:25882909</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
[[Category: Ermler, U]] | [[Category: Ermler, U]] | ||
[[Category: Fujishiro, T]] | [[Category: Fujishiro, T]] | ||
| + | [[Category: Shima, S]] | ||
| + | [[Category: Adenylyltransferase]] | ||
| + | [[Category: Atp binding]] | ||
| + | [[Category: E1 enzyme superfamily]] | ||
| + | [[Category: Transferase]] | ||
| + | [[Category: Uba/thif-type nad/fad binding fold]] | ||
Revision as of 11:31, 30 April 2015
ATP-bound HcgE from Methanothermobacter marburgensis
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