9r52
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Dimeric state of the F420-reducing hydrogenase from Methanothermococcus thermolithotrophicus in crystalline form 2== | |
| + | <StructureSection load='9r52' size='340' side='right'caption='[[9r52]], [[Resolution|resolution]] 1.65Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[9r52]] is a 3 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=9R52 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9R52 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]] 1.65Å</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=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NFU:FORMYL[BIS(HYDROCYANATO-1KAPPAC)]IRONNICKEL(FE-NI)'>NFU</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=9r52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9r52 OCA], [https://pdbe.org/9r52 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9r52 RCSB], [https://www.ebi.ac.uk/pdbsum/9r52 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9r52 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: | + | <div class="pdbe-citations 9r52" style="background-color:#fffaf0;"></div> |
| - | [[Category: Jespersen | + | == References == |
| - | [[Category: Wagner | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Methanothermococcus thermolithotrophicus DSM 2095]] | ||
| + | [[Category: Jespersen M]] | ||
| + | [[Category: Lemaire ON]] | ||
| + | [[Category: Wagner T]] | ||
Current revision
Dimeric state of the F420-reducing hydrogenase from Methanothermococcus thermolithotrophicus in crystalline form 2
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