9r6z: Difference between revisions
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==Cubic state of the F420-reducing hydrogenase from Methanothermococcus thermolithotrophicus== | |||
<StructureSection load='9r6z' size='340' side='right'caption='[[9r6z]], [[Resolution|resolution]] 2.85Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9r6z]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanothermococcus_thermolithotrophicus_DSM_2095 Methanothermococcus thermolithotrophicus DSM 2095]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9R6Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9R6Z 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]] 2.85Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NFU:FORMYL[BIS(HYDROCYANATO-1KAPPAC)]IRONNICKEL(FE-NI)'>NFU</scene>, <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=9r6z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9r6z OCA], [https://pdbe.org/9r6z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9r6z RCSB], [https://www.ebi.ac.uk/pdbsum/9r6z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9r6z ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Hydrogenases catalyze reversible H(2) production and are potential models for renewable energy catalysts. Here, the full redox landscape of a group 3 [NiFe]-hydrogenase from methanothermococcus thermolithotrophicus is elucidated, resembling group 1 enzymes. Structural and spectroscopic analyses reveal a catalytic-ready state with nickel seesaw coordination, enabling intermediate trapping and advancing mechanistic understanding of oxygen-sensitive [NiFe] enzymes. | |||
Structural and Spectroscopic Insights into Catalytic Intermediates of a [NiFe]-hydrogenase from Group 3.,Jespersen M, Lorent C, Lemaire ON, Zebger I, Wagner T Chembiochem. 2025 Oct 13:e202500692. doi: 10.1002/cbic.202500692. PMID:41078086<ref>PMID:41078086</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Jespersen | <div class="pdbe-citations 9r6z" style="background-color:#fffaf0;"></div> | ||
[[Category: Lemaire | == References == | ||
[[Category: Wagner | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Methanothermococcus thermolithotrophicus DSM 2095]] | |||
[[Category: Jespersen M]] | |||
[[Category: Lemaire ON]] | |||
[[Category: Wagner T]] | |||
Latest revision as of 09:24, 22 October 2025
Cubic state of the F420-reducing hydrogenase from Methanothermococcus thermolithotrophicus
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