| Structural highlights
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.
| | Ligands: | , |
| Gene: | PFC_06375 (Pyrococcus furiosus COM1), PFC_06345 (Pyrococcus furiosus COM1), mbhJ, mbh10, PF1432 (PYRFU), mbhK, mbh11, PF1433 (PYRFU), mbhL, mbh12, PF1434 (PYRFU), PFC_06405 (Pyrococcus furiosus COM1), PFC_06370 (Pyrococcus furiosus COM1), PF1426 (PYRFU), PFC_06380 (Pyrococcus furiosus COM1), PFC_06400 (Pyrococcus furiosus COM1), PFC_06365 (Pyrococcus furiosus COM1), PFC_06340 (Pyrococcus furiosus COM1), PFC_06360 (Pyrococcus furiosus COM1), PFC_06350 (Pyrococcus furiosus COM1) |
| Activity: | Ferredoxin hydrogenase, with EC number 1.12.7.2 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[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
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