5nf8

From Proteopedia

(Difference between revisions)

Current revision

Solution structure of detergent-solubilized Rcf1, a yeast mitochondrial inner membrane protein involved in respiratory Complex III/IV supercomplex formation

Structural highlights

5nf8 is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RCF1_YEAST Assembly factor that plays a role in the assembly of the respiratory chain supercomplexes (SCs) composed of ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV). Involved in the recruitment of COX13 and RCF2 into cytochrome c oxidase. May also be required for late-stage assembly of the COX12 and COX13 subunits (PubMed:22310663, PubMed:22342701, PubMed:22405070). Required for the generation and maintenance of a normal proton motive force (PMF) across the inner mitochondrial membrane (IMM) by preventing proton leakage through an inactive population of CIV that accumulates when RCF1 and/or RCF2 proteins are absent (PubMed:30683696, PubMed:31591265).^[1] ^[2] ^[3] ^[4] ^[5]

Publication Abstract from PubMed

The Saccharomyces cerevisiae respiratory supercomplex factor 1 (Rcf1) protein is located in the mitochondrial inner membrane where it is involved in formation of supercomplexes composed of respiratory complexes III and IV. We report the solution structure of Rcf1, which forms a dimer in dodecylphosphocholine (DPC) micelles, where each monomer consists of a bundle of five transmembrane (TM) helices and a short flexible soluble helix (SH). Three TM helices are unusually charged and provide the dimerization interface consisting of 10 putative salt bridges, defining a "charge zipper" motif. The dimer structure is supported by molecular dynamics (MD) simulations in DPC, although the simulations show a more dynamic dimer interface than the NMR data. Furthermore, CD and NMR data indicate that Rcf1 undergoes a structural change when reconstituted in liposomes, which is supported by MD data, suggesting that the dimer structure is unstable in a planar membrane environment. Collectively, these data indicate a dynamic monomer-dimer equilibrium. Furthermore, the Rcf1 dimer interacts with cytochrome c, suggesting a role as an electron-transfer bridge between complexes III and IV. The Rcf1 structure will help in understanding its functional roles at a molecular level.

Solution NMR structure of yeast Rcf1, a protein involved in respiratory supercomplex formation.,Zhou S, Pettersson P, Huang J, Sjoholm J, Sjostrand D, Pomes R, Hogbom M, Brzezinski P, Maler L, Adelroth P Proc Natl Acad Sci U S A. 2018 Mar 5. pii: 1712061115. doi:, 10.1073/pnas.1712061115. PMID:29507228^[6]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Strogolova V, Furness A, Robb-McGrath M, Garlich J, Stuart RA. Rcf1 and Rcf2, members of the hypoxia-induced gene 1 protein family, are critical components of the mitochondrial cytochrome bc1-cytochrome c oxidase supercomplex. Mol Cell Biol. 2012 Apr;32(8):1363-73. doi: 10.1128/MCB.06369-11. Epub 2012 Feb, 6. PMID:22310663 doi:http://dx.doi.org/10.1128/MCB.06369-11
↑ Vukotic M, Oeljeklaus S, Wiese S, Vogtle FN, Meisinger C, Meyer HE, Zieseniss A, Katschinski DM, Jans DC, Jakobs S, Warscheid B, Rehling P, Deckers M. Rcf1 mediates cytochrome oxidase assembly and respirasome formation, revealing heterogeneity of the enzyme complex. Cell Metab. 2012 Mar 7;15(3):336-47. doi: 10.1016/j.cmet.2012.01.016. Epub 2012, Feb 16. PMID:22342701 doi:http://dx.doi.org/10.1016/j.cmet.2012.01.016
↑ Chen YC, Taylor EB, Dephoure N, Heo JM, Tonhato A, Papandreou I, Nath N, Denko NC, Gygi SP, Rutter J. Identification of a protein mediating respiratory supercomplex stability. Cell Metab. 2012 Mar 7;15(3):348-60. PMID:22405070 doi:10.1016/j.cmet.2012.02.006
↑ Strogolova V, Hoang NH, Hosler J, Stuart RA. The yeast mitochondrial proteins Rcf1 and Rcf2 support the enzymology of the cytochrome c oxidase complex and generation of the proton motive force. J Biol Chem. 2019 Mar 29;294(13):4867-4877. doi: 10.1074/jbc.RA118.006888. Epub, 2019 Jan 25. PMID:30683696 doi:http://dx.doi.org/10.1074/jbc.RA118.006888
↑ Hoang NH, Strogolova V, Mosley JJ, Stuart RA, Hosler J. Hypoxia-inducible gene domain 1 proteins in yeast mitochondria protect against proton leak through complex IV. J Biol Chem. 2019 Nov 15;294(46):17669-17677. doi: 10.1074/jbc.RA119.010317. Epub, 2019 Oct 7. PMID:31591265 doi:http://dx.doi.org/10.1074/jbc.RA119.010317
↑ Zhou S, Pettersson P, Huang J, Sjoholm J, Sjostrand D, Pomes R, Hogbom M, Brzezinski P, Maler L, Adelroth P. Solution NMR structure of yeast Rcf1, a protein involved in respiratory supercomplex formation. Proc Natl Acad Sci U S A. 2018 Mar 5. pii: 1712061115. doi:, 10.1073/pnas.1712061115. PMID:29507228 doi:http://dx.doi.org/10.1073/pnas.1712061115

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/5nf8"

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[5nf8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NF8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NF8 FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5nf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nf8 OCA], [https://pdbe.org/5nf8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nf8 RCSB], [https://www.ebi.ac.uk/pdbsum/5nf8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nf8 ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5nf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nf8 OCA], [https://pdbe.org/5nf8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nf8 RCSB], [https://www.ebi.ac.uk/pdbsum/5nf8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nf8 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[https://www.uniprot.org/uniprot/RCF1_YEAST RCF1_YEAST] Assembly factor that plays a role in the assembly of the respiratory chain supercomplexes (SCs) composed of ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV). Involved in the recruitment of COX13 and RCF2 into cytochrome c oxidase. May also be required for late-stage assembly of the COX12 and COX13 subunits (PubMed:22342701, PubMed:22405070, PubMed:22310663). Required for the generation and maintenance of a normal proton motive force (PMF) across the inner mitochondrial membrane (IMM) by preventing proton leakage through an inactive population of CIV that accumulates when RCF1 and/or RCF2 proteins are absent (PubMed:30683696, PubMed:31591265).<ref>PMID:22310663</ref> <ref>PMID:22342701</ref> <ref>PMID:22405070</ref> <ref>PMID:30683696</ref> <ref>PMID:31591265</ref>
+[https://www.uniprot.org/uniprot/RCF1_YEAST RCF1_YEAST] Assembly factor that plays a role in the assembly of the respiratory chain supercomplexes (SCs) composed of ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV). Involved in the recruitment of COX13 and RCF2 into cytochrome c oxidase. May also be required for late-stage assembly of the COX12 and COX13 subunits (PubMed:22310663, PubMed:22342701, PubMed:22405070). Required for the generation and maintenance of a normal proton motive force (PMF) across the inner mitochondrial membrane (IMM) by preventing proton leakage through an inactive population of CIV that accumulates when RCF1 and/or RCF2 proteins are absent (PubMed:30683696, PubMed:31591265).<ref>PMID:22310663</ref> <ref>PMID:22342701</ref> <ref>PMID:22405070</ref> <ref>PMID:30683696</ref> <ref>PMID:31591265</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

5nf8

From Proteopedia

Current revision

Solution structure of detergent-solubilized Rcf1, a yeast mitochondrial inner membrane protein involved in respiratory Complex III/IV supercomplex formation

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox