6cfw

From Proteopedia

(Difference between revisions)

Revision as of 05:55, 27 June 2018

cryoEM structure of a respiratory membrane-bound hydrogenase

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6cfw"

@@ Line 3: / Line 3: @@
 <StructureSection load='6cfw' size='340' side='right' caption='[[6cfw]], [[Resolution|resolution]] 3.70&Aring;' 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>
+<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>
 </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PFC_06375 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1185654 Pyrococcus furiosus COM1]), PFC_06345 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1185654 Pyrococcus furiosus COM1]), mbhJ, mbh10, PF1432 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=186497 PYRFU]), mbhK, mbh11, PF1433 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=186497 PYRFU]), mbhL, mbh12, PF1434 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=186497 PYRFU]), PFC_06405 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1185654 Pyrococcus furiosus COM1]), PFC_06370 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1185654 Pyrococcus furiosus COM1]), PF1426 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=186497 PYRFU]), PFC_06380 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1185654 Pyrococcus furiosus COM1]), PFC_06400 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1185654 Pyrococcus furiosus COM1]), PFC_06365 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1185654 Pyrococcus furiosus COM1]), PFC_06340 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1185654 Pyrococcus furiosus COM1]), PFC_06360 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1185654 Pyrococcus furiosus COM1]), PFC_06350 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1185654 Pyrococcus furiosus COM1])</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>
@@ Line 24: / Line 25: @@
 </StructureSection>
 [[Category: Ferredoxin hydrogenase]]
+[[Category: Pyrfu]]
+[[Category: Pyrococcus furiosus com1]]
 [[Category: Li, H L]]
 [[Category: Yu, H J]]

6cfw

From Proteopedia

Revision as of 05:55, 27 June 2018

cryoEM structure of a respiratory membrane-bound hydrogenase

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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