4jjf: Difference between revisions
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==Crystal structure of FE-hydrogenase from methanothermobacter marburgensis in complex with 2-naphthylisocyanide== | |||
<StructureSection load='4jjf' size='340' side='right' caption='[[4jjf]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4jjf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_marburgensis Methanothermobacter marburgensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JJF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JJF FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE9:IRON-GUANYLYL+PYRIDINOL+COFACTOR'>FE9</scene>, <scene name='pdbligand=N2I:N-(NAPHTHALEN-2-YL)METHANIMINE'>N2I</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2boj|2boj]], [[3daf|3daf]], [[3dag|3dag]], [[3f46|3f46]], [[3f47|3f47]]</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/5,10-methenyltetrahydromethanopterin_hydrogenase 5,10-methenyltetrahydromethanopterin hydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.12.98.2 1.12.98.2] </span></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=4jjf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jjf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4jjf RCSB], [http://www.ebi.ac.uk/pdbsum/4jjf PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Inhibition mechanism: Isocyanides strongly inhibit [Fe]-hydrogenase. X-ray crystallography and X-ray absorption spectroscopy revealed that the isocyanide binds to the trans position, versus the acyl carbon of the Fe center, and is covalently bound to the pyridinol hydroxy oxygen. These results also indicated that the hydroxy group is essential for H2 activation. | |||
Crystal Structures of [Fe]-Hydrogenase in Complex with Inhibitory Isocyanides: Implications for the H -Activation Site.,Tamura H, Salomone-Stagni M, Fujishiro T, Warkentin E, Meyer-Klaucke W, Ermler U, Shima S Angew Chem Int Ed Engl. 2013 Jul 22. doi: 10.1002/anie.201305089. PMID:23873755<ref>PMID:23873755</ref> | |||
[ | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: 5,10-methenyltetrahydromethanopterin hydrogenase]] | [[Category: 5,10-methenyltetrahydromethanopterin hydrogenase]] | ||
[[Category: Methanothermobacter marburgensis]] | [[Category: Methanothermobacter marburgensis]] | ||
[[Category: Ermler, U | [[Category: Ermler, U]] | ||
[[Category: Shima, S | [[Category: Shima, S]] | ||
[[Category: Tamura, H | [[Category: Tamura, H]] | ||
[[Category: Warkentin, E | [[Category: Warkentin, E]] | ||
[[Category: Alpha-beta fold]] | [[Category: Alpha-beta fold]] | ||
[[Category: Hydrogenase]] | [[Category: Hydrogenase]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
