6sg2
From Proteopedia
(Difference between revisions)
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==FeFe Hydrogenase from Desulfovibrio desulfuricans in Hinact state== | ==FeFe Hydrogenase from Desulfovibrio desulfuricans in Hinact state== | ||
| - | <StructureSection load='6sg2' size='340' side='right'caption='[[6sg2]]' scene=''> | + | <StructureSection load='6sg2' size='340' side='right'caption='[[6sg2]], [[Resolution|resolution]] 1.65Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SG2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6SG2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6sg2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_desulfuricans"_(beijerinck_1895)_saltet_1900 "bacillus desulfuricans" (beijerinck 1895) saltet 1900]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SG2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6SG2 FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6sg2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sg2 OCA], [http://pdbe.org/6sg2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6sg2 RCSB], [http://www.ebi.ac.uk/pdbsum/6sg2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6sg2 ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LFH:dicarbonyl[bis(cyanide-kappaC)]-mu-(iminodimethanethiolatato-1kappaS 2kappaS)-mu-(oxomethylidene)diiron(2+)+sulphide'>LFH</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr> |
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hydA, DDE01_08480 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=876 "Bacillus desulfuricans" (Beijerinck 1895) Saltet 1900])</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6sg2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sg2 OCA], [http://pdbe.org/6sg2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6sg2 RCSB], [http://www.ebi.ac.uk/pdbsum/6sg2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6sg2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | [FeFe] hydrogenases are the most active H 2 converting catalysts in nature but their extreme oxygen sensitivity limits their use in technological applications. The [FeFe] hydrogenases from sulfate reducing bacteria can be purified in an O 2 -stable state called H inact . To date, the structure and mechanism of formation of H inact remain unknown. Our 1.65 A crystal structure of this state reveals a sulfur ligand bound to the open coordination site. Furthermore, in-depth spectroscopic characterization by X-ray absorption spectroscopy (XAS), nuclear resonance vibrational spectroscopy (NRVS), resonance Raman (RR) spectroscopy and infrared (IR) spectroscopy, together with hybrid quantum mechanical and molecular mechanical (QM/MM) calculations, provide detailed chemical insight into the H inact state and its mechanism of formation. This may facilitate the design of O 2 -stable hydrogenases and molecular catalysts. | ||
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| + | Caught in the Hinact: Crystal Structure and Spectroscopy Reveal a Sulfur Bound to the Active Site of an O2-stable State of [FeFe] Hydrogenase.,Rodriguez-Macia P, Galle L, Bjornsson R, Lorent C, Zebger I, Yoda Y, Cramer S, DeBeer S, Span I, Birrell J Angew Chem Int Ed Engl. 2020 Jun 2. doi: 10.1002/anie.202005208. PMID:32488975<ref>PMID:32488975</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6sg2" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Galle | + | [[Category: Galle, L M]] |
| - | [[Category: Span I]] | + | [[Category: Span, I]] |
| + | [[Category: Desulfovibrio desulfurican]] | ||
| + | [[Category: Hinact]] | ||
| + | [[Category: Hydrogenase]] | ||
| + | [[Category: Iron-sulfur protein]] | ||
| + | [[Category: Oxidoreductase]] | ||
Revision as of 07:34, 30 September 2020
FeFe Hydrogenase from Desulfovibrio desulfuricans in Hinact state
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