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-Structure paper
タイトル | Cryo-EM structure and function of S. pombe complex IV with bound respiratory supercomplex factor. |
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ジャーナル・号・ページ | Commun Chem, Vol. 6, Issue 1, Page 32, Year 2023 |
掲載日 | 2023年2月16日 |
著者 | Agnes Moe / Pia Ädelroth / Peter Brzezinski / Linda Näsvik Öjemyr / |
PubMed 要旨 | Fission yeast Schizosaccharomyces pombe serves as model organism for studying higher eukaryotes. We combined the use of cryo-EM and spectroscopy to investigate the structure and function of affinity ...Fission yeast Schizosaccharomyces pombe serves as model organism for studying higher eukaryotes. We combined the use of cryo-EM and spectroscopy to investigate the structure and function of affinity purified respiratory complex IV (CIV) from S. pombe. The reaction sequence of the reduced enzyme with O proceeds over a time scale of µs-ms, similar to that of the mammalian CIV. The cryo-EM structure of CIV revealed eleven subunits as well as a bound hypoxia-induced gene 1 (Hig1) domain of respiratory supercomplex factor 2 (Rcf2). These results suggest that binding of Rcf2 does not require the presence of a CIII-CIV supercomplex, i.e. Rcf2 is a component of CIV. An AlphaFold-Multimer model suggests that the Hig1 domains of both Rcf1 and Rcf2 bind at the same site of CIV suggesting that their binding is mutually exclusive. Furthermore, the differential functional effect of Rcf1 or Rcf2 is presumably caused by interactions of CIV with their different non-Hig1 domain parts. |
リンク | Commun Chem / PubMed:36797353 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.36 Å |
構造データ | EMDB-16491, PDB-8c8q: |
化合物 | ChemComp-HEA: ChemComp-CU: ChemComp-MG: ChemComp-CA: ChemComp-PEF: ChemComp-CUA: ChemComp-ZN: |
由来 |
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キーワード | MEMBRANE PROTEIN / Electron transfer / proton transfer / respiration |