This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
<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>
Line 23:
Line 23:
<references/>
<references/>
__TOC__
__TOC__
-
</StructureSection>
+
</SX>
[[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
