6ttl
From Proteopedia
(Difference between revisions)
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==crystal structure of [FeFe]-hydrogenase CbA5H (partial) from Clostridium beijerinckii in Hinact state== | ==crystal structure of [FeFe]-hydrogenase CbA5H (partial) from Clostridium beijerinckii in Hinact state== | ||
| - | <StructureSection load='6ttl' size='340' side='right'caption='[[6ttl]]' scene=''> | + | <StructureSection load='6ttl' size='340' side='right'caption='[[6ttl]], [[Resolution|resolution]] 2.90Å' 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=6TTL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TTL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6ttl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_beijerinckii Clostridium beijerinckii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TTL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TTL FirstGlance]. <br> |
| - | </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=6ttl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ttl OCA], [https://pdbe.org/6ttl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ttl RCSB], [https://www.ebi.ac.uk/pdbsum/6ttl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ttl ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=402:DICARBONYL[BIS(CYANIDE-KAPPAC)]-MU-(IMINODIMETHANETHIOLATATO-1KAPPAS 2KAPPAS)-MU-(OXOMETHYLIDENE)DIIRON(2+)'>402</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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=6ttl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ttl OCA], [https://pdbe.org/6ttl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ttl RCSB], [https://www.ebi.ac.uk/pdbsum/6ttl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ttl ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A1I9RYV3_CLOBE A0A1I9RYV3_CLOBE] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | [FeFe]-hydrogenases are efficient H(2)-catalysts, yet upon contact with dioxygen their catalytic cofactor (H-cluster) is irreversibly inactivated. Here, we combine X-ray crystallography, rational protein design, direct electrochemistry, and Fourier-transform infrared spectroscopy to describe a protein morphing mechanism that controls the reversible transition between the catalytic H(ox)-state and the inactive but oxygen-resistant H(inact)-state in [FeFe]-hydrogenase CbA5H of Clostridium beijerinckii. The X-ray structure of air-exposed CbA5H reveals that a conserved cysteine residue in the local environment of the active site (H-cluster) directly coordinates the substrate-binding site, providing a safety cap that prevents O(2)-binding and consequently, cofactor degradation. This protection mechanism depends on three non-conserved amino acids situated approximately 13 A away from the H-cluster, demonstrating that the 1st coordination sphere chemistry of the H-cluster can be remote-controlled by distant residues. | ||
| + | |||
| + | A safety cap protects hydrogenase from oxygen attack.,Winkler M, Duan J, Rutz A, Felbek C, Scholtysek L, Lampret O, Jaenecke J, Apfel UP, Gilardi G, Valetti F, Fourmond V, Hofmann E, Leger C, Happe T Nat Commun. 2021 Feb 2;12(1):756. doi: 10.1038/s41467-020-20861-2. PMID:33531463<ref>PMID:33531463</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6ttl" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Clostridium beijerinckii]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Duan J]] | [[Category: Duan J]] | ||
Current revision
crystal structure of [FeFe]-hydrogenase CbA5H (partial) from Clostridium beijerinckii in Hinact state
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