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==Cryo-EM structure of the F420-reducing NiFe-hydrogenase from a methanogenic archaeon with bound substrate== | ==Cryo-EM structure of the F420-reducing NiFe-hydrogenase from a methanogenic archaeon with bound substrate== | ||
<StructureSection load='3zfs' size='340' side='right' caption='[[3zfs]], [[Resolution|resolution]] 4.00Å' scene=''> | <StructureSection load='3zfs' size='340' side='right' caption='[[3zfs]], [[Resolution|resolution]] 4.00Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=F42:COENZYME+F420'>F42</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FCO:CARBONMONOXIDE-(DICYANO)+IRON'>FCO</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=F42:COENZYME+F420'>F42</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FCO:CARBONMONOXIDE-(DICYANO)+IRON'>FCO</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Coenzyme_F420_hydrogenase Coenzyme F420 hydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.12.98.1 1.12.98.1] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Coenzyme_F420_hydrogenase Coenzyme F420 hydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.12.98.1 1.12.98.1] </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=3zfs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zfs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zfs RCSB], [http://www.ebi.ac.uk/pdbsum/3zfs PDBsum]</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=3zfs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zfs OCA], [http://pdbe.org/3zfs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3zfs RCSB], [http://www.ebi.ac.uk/pdbsum/3zfs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3zfs ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3zfs" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 22:15, 11 August 2016
Cryo-EM structure of the F420-reducing NiFe-hydrogenase from a methanogenic archaeon with bound substrateCryo-EM structure of the F420-reducing NiFe-hydrogenase from a methanogenic archaeon with bound substrate
Structural highlights
Publication Abstract from PubMedMethanogenic archaea use a [NiFe]-hydrogenase, Frh, for oxidation/reduction of F, an important hydride carrier in the methanogenesis pathway from H and CO. Frh accounts for about 1% of the cytoplasmic protein and forms a huge complex consisting of FrhABG heterotrimers with each a [NiFe] center, four Fe-S clusters and an FAD. Here, we report the structure determined by near-atomic resolution cryo-EM of Frh with and without bound substrate F. The polypeptide chains of FrhB, for which there was no homolog, was traced de novo from the EM map. The 1.2-MDa complex contains 12 copies of the heterotrimer, which unexpectedly form a spherical protein shell with a hollow core. The cryo-EM map reveals strong electron density of the chains of metal clusters running parallel to the protein shell, and the F-binding site is located at the end of the chain near the outside of the spherical structure. http://dx.doi.org/10.7554/eLife.00218.001. De novo modeling of the F420-reducing [NiFe]-hydrogenase from a methanogenic archaeon by cryo-electron microscopy.,Mills DJ, Vitt S, Strauss M, Shima S, Vonck J Elife. 2013;2:e00218. doi: 10.7554/eLife.00218. Epub 2013 Mar 5. PMID:23483797[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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