Crystal structure of the alternative complex III from the phototrophic bacterium Chloroflexus aurantiacus

被引:1
|
作者
Wu, Wenping [1 ]
Fang, Han [1 ]
He, Huimin [2 ]
Wu, Jingyi [1 ]
Gong, Zijun [1 ]
Li, Chunyang [1 ]
Pei, Xinkai [1 ]
Xu, Xiaoling [1 ,2 ,3 ]
机构
[1] Hangzhou Normal Univ, Sch Basic Med Sci, Dept Biochem & Mol Biol, Zhejiang Key Lab Med Epigenet, Hangzhou 311121, Peoples R China
[2] Hangzhou Normal Univ, Coll Life & Environm Sci, Photosynth Res Ctr, Hangzhou 311121, Peoples R China
[3] Zhejiang Univ, Affiliated Hosp 2, Coll Med, Dept Cardiol,Cardiovasc Key Lab Zhejiang Prov, Hangzhou 310009, Peoples R China
关键词
ELECTRON-TRANSFER CHAIN; RHODOTHERMUS-MARINUS; CYTOCHROME BC; CRYO-EM; FLEXIBILITY;
D O I
10.1016/j.str.2024.10.014
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Alternative complex III (ACIII) is a multi-subunit quinol:electron acceptor oxidoreductase that couples quinol oxidation with transmembrane proton translocation in bacterial respiratory and photosynthetic electron transport chains. Four ACIII cryoelectron microscopy (cryo-EM) structures are known. However, the effects of cryo-EM versus X-ray crystallography structure determination on ACIII structure are unclear. Here, we report a 3.25 A & ring; crystal structure of photosynthetic ACIII from Chloroflexus aurantiacus (CaACIIIp), revealing eight subunits (ActA-G and I) with four iron-sulfur clusters and six c-type hemes, a menaquinol-binding site, and two proton translocation passages. Structural comparisons with the previously reported cryo-EM structures reveal slight local conformational changes in the solvent-exposed regions of ActB, ActD, ActG, and the transmembrane (TM) helix of subunit I. The regions conferring structural flexibility possess low sequence conservation across species. However, the core functional modules containing the menaquinol-binding pocket, redox centers, and proton translocation passages remain unchanged, preserving the enzyme's activity.
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页数:13
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