6cfw
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==cryoEM structure of a respiratory membrane-bound hydrogenase== | |
| + | <StructureSection load='6cfw' size='340' side='right' caption='[[6cfw]], [[Resolution|resolution]] 3.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6cfw]] is a 14 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CFW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CFW FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NFU:FORMYL[BIS(HYDROCYANATO-1KAPPAC)]IRONNICKEL(FE-NI)'>NFU</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/Ferredoxin_hydrogenase Ferredoxin hydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.12.7.2 1.12.7.2] </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=6cfw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cfw OCA], [http://pdbe.org/6cfw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cfw RCSB], [http://www.ebi.ac.uk/pdbsum/6cfw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cfw ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/MBHJ_PYRFU MBHJ_PYRFU]] Probable subunit of a hydrogen-evolving hydrogenase that utilizes protons both as a substrate for hydrogen production and proton translocation. Acts by coupling the redox reaction via ferredoxin and iron-sulfur (Fe-S) clusters to proton translocation across the membrane, thereby conserving the redox energy in a proton gradient.<ref>PMID:10852873</ref> <ref>PMID:11054105</ref> <ref>PMID:12792025</ref> [[http://www.uniprot.org/uniprot/MBHLB_PYRFU MBHLB_PYRFU]] Beta subunit of a hydrogen-evolving hydrogenase that utilizes protons both as a substrate for hydrogen production and proton translocation. Acts by coupling the redox reaction via ferredoxin and iron-sulfur (Fe-S) clusters to proton translocation across the membrane thereby conserving the redox energy in a proton gradient.<ref>PMID:10852873</ref> <ref>PMID:11054105</ref> <ref>PMID:12792025</ref> [[http://www.uniprot.org/uniprot/MBHLA_PYRFU MBHLA_PYRFU]] Alpha subunit of a hydrogen-evolving hydrogenase that utilizes protons both as a substrate for hydrogen production and proton translocation. Acts by coupling the redox reaction via ferredoxin and iron-sulfur (Fe-S) clusters to proton translocation across the membrane thereby conserving the redox energy in a proton gradient.<ref>PMID:10852873</ref> <ref>PMID:11054105</ref> <ref>PMID:12792025</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Hydrogen gas-evolving membrane-bound hydrogenase (MBH) and quinone-reducing complex I are homologous respiratory complexes with a common ancestor, but a structural basis for their evolutionary relationship is lacking. Here, we report the cryo-EM structure of a 14-subunit MBH from the hyperthermophile Pyrococcus furiosus. MBH contains a membrane-anchored hydrogenase module that is highly similar structurally to the quinone-binding Q-module of complex I while its membrane-embedded ion-translocation module can be divided into a H(+)- and a Na(+)-translocating unit. The H(+)-translocating unit is rotated 180 degrees in-membrane with respect to its counterpart in complex I, leading to distinctive architectures for the two respiratory systems despite their largely conserved proton-pumping mechanisms. The Na(+)-translocating unit, absent in complex I, resembles that found in the Mrp H(+)/Na(+) antiporter and enables hydrogen gas evolution by MBH to establish a Na(+) gradient for ATP synthesis near 100 degrees C. MBH also provides insights into Mrp structure and evolution of MBH-based respiratory enzymes. | ||
| - | + | Structure of an Ancient Respiratory System.,Yu H, Wu CH, Schut GJ, Haja DK, Zhao G, Peters JW, Adams MWW, Li H Cell. 2018 Apr 25. pii: S0092-8674(18)30403-3. doi: 10.1016/j.cell.2018.03.071. PMID:29754813<ref>PMID:29754813</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6cfw" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Ferredoxin hydrogenase]] | ||
| + | [[Category: Li, H L]] | ||
| + | [[Category: Yu, H J]] | ||
| + | [[Category: Hydrogenase]] | ||
| + | [[Category: Ion translocation]] | ||
| + | [[Category: Membrane protein]] | ||
| + | [[Category: Respiratory]] | ||
Revision as of 07:24, 23 May 2018
cryoEM structure of a respiratory membrane-bound hydrogenase
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