5nf8
From Proteopedia
(Difference between revisions)
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<StructureSection load='5nf8' size='340' side='right' caption='[[5nf8]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''> | <StructureSection load='5nf8' size='340' side='right' caption='[[5nf8]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5nf8]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NF8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5nf8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. 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 [http://oca.weizmann.ac.il/oca-docs/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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5nf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nf8 OCA], [http://pdbe.org/5nf8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nf8 RCSB], [http://www.ebi.ac.uk/pdbsum/5nf8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nf8 ProSAT]</span></td></tr> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RCF1, AIM31, SCRG_01865 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=5nf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nf8 OCA], [http://pdbe.org/5nf8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nf8 RCSB], [http://www.ebi.ac.uk/pdbsum/5nf8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nf8 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/RCF1_YEAS1 RCF1_YEAS1]] Cytochrome c oxidase subunit required for growth under hypoxic conditions. Involved in the assembly of the Complex III-Complex IV supercomplex, as well as 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 and for cytochrome c oxidase activity (By similarity). | [[http://www.uniprot.org/uniprot/RCF1_YEAS1 RCF1_YEAS1]] Cytochrome c oxidase subunit required for growth under hypoxic conditions. Involved in the assembly of the Complex III-Complex IV supercomplex, as well as 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 and for cytochrome c oxidase activity (By similarity). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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. | ||
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| + | 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<ref>PMID:29507228</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5nf8" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Atcc 18824]] | ||
[[Category: Adelroth, P]] | [[Category: Adelroth, P]] | ||
[[Category: Brzezinski, P]] | [[Category: Brzezinski, P]] | ||
Revision as of 06:49, 14 March 2018
Solution structure of detergent-solubilized Rcf1, a yeast mitochondrial inner membrane protein involved in respiratory Complex III/IV supercomplex formation
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