<table><tr><td colspan='2'>[[6cfw]] is a 14 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrfu Pyrfu] and [http://en.wikipedia.org/wiki/Pyrococcus_furiosus_com1 Pyrococcus furiosus com1]. 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>
<table><tr><td colspan='2'>[[6cfw]] is a 14 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrfu Pyrfu] and [http://en.wikipedia.org/wiki/Pyrococcus_furiosus_com1 Pyrococcus furiosus com1]. 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>
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[[Category: Ferredoxin hydrogenase]]
[[Category: Ferredoxin hydrogenase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
Revision as of 20:40, 6 March 2020
cryoEM structure of a respiratory membrane-bound hydrogenase
6cfw is a 14 chain structure with sequence from Pyrfu and Pyrococcus furiosus com1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
[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.[1][2][3] [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.[4][5][6] [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.[7][8][9]
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[10]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Sapra R, Verhagen MF, Adams MW. Purification and characterization of a membrane-bound hydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus. J Bacteriol. 2000 Jun;182(12):3423-8. PMID:10852873
↑ Silva PJ, van den Ban EC, Wassink H, Haaker H, de Castro B, Robb FT, Hagen WR. Enzymes of hydrogen metabolism in Pyrococcus furiosus. Eur J Biochem. 2000 Nov;267(22):6541-51. PMID:11054105
↑ Sapra R, Bagramyan K, Adams MW. A simple energy-conserving system: proton reduction coupled to proton translocation. Proc Natl Acad Sci U S A. 2003 Jun 24;100(13):7545-50. doi:, 10.1073/pnas.1331436100. Epub 2003 Jun 5. PMID:12792025 doi:http://dx.doi.org/10.1073/pnas.1331436100
↑ Sapra R, Verhagen MF, Adams MW. Purification and characterization of a membrane-bound hydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus. J Bacteriol. 2000 Jun;182(12):3423-8. PMID:10852873
↑ Silva PJ, van den Ban EC, Wassink H, Haaker H, de Castro B, Robb FT, Hagen WR. Enzymes of hydrogen metabolism in Pyrococcus furiosus. Eur J Biochem. 2000 Nov;267(22):6541-51. PMID:11054105
↑ Sapra R, Bagramyan K, Adams MW. A simple energy-conserving system: proton reduction coupled to proton translocation. Proc Natl Acad Sci U S A. 2003 Jun 24;100(13):7545-50. doi:, 10.1073/pnas.1331436100. Epub 2003 Jun 5. PMID:12792025 doi:http://dx.doi.org/10.1073/pnas.1331436100
↑ Sapra R, Verhagen MF, Adams MW. Purification and characterization of a membrane-bound hydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus. J Bacteriol. 2000 Jun;182(12):3423-8. PMID:10852873
↑ Silva PJ, van den Ban EC, Wassink H, Haaker H, de Castro B, Robb FT, Hagen WR. Enzymes of hydrogen metabolism in Pyrococcus furiosus. Eur J Biochem. 2000 Nov;267(22):6541-51. PMID:11054105
↑ Sapra R, Bagramyan K, Adams MW. A simple energy-conserving system: proton reduction coupled to proton translocation. Proc Natl Acad Sci U S A. 2003 Jun 24;100(13):7545-50. doi:, 10.1073/pnas.1331436100. Epub 2003 Jun 5. PMID:12792025 doi:http://dx.doi.org/10.1073/pnas.1331436100
↑ Yu H, Wu CH, Schut GJ, Haja DK, Zhao G, Peters JW, Adams MWW, Li H. Structure of an Ancient Respiratory System. Cell. 2018 Apr 25. pii: S0092-8674(18)30403-3. doi: 10.1016/j.cell.2018.03.071. PMID:29754813 doi:http://dx.doi.org/10.1016/j.cell.2018.03.071
