期刊
OPEN BIOLOGY
卷 5, 期 9, 页码 -出版社
ROYAL SOC
DOI: 10.1098/rsob.150119
关键词
alpha-proteobacteria; Paracoccus denitrificans; F-ATPase; subunits; cardiolipin; crystallization
资金
- Medical Research Council via MRC [U105663150]
- Biotechnology and Biological Sciences Research Council
- Medical Research Council [MC_EX_MR/M009858/1] Funding Source: researchfish
- MRC [MC_EX_MR/M009858/1] Funding Source: UKRI
The structures of F-ATPases have been determined predominantly with mitochondrial enzymes, but hitherto no F-ATPase has been crystallized intact. A high-resolution model of the bovine enzyme built up from separate substructures determined by X-ray crystallography contains about 85% of the entire complex, but it lacks a crucial region that provides a transmembrane proton pathway involved in the generation of the rotary mechanism that drives the synthesis of ATP. Here the isolation, characterization and crystallization of an integral F-ATPase complex from the alpha-proteobacterium Paracoccus denitrificans are described. Unlike many eubacterial F-ATPases, which can both synthesize and hydrolyse ATP, the P. denitrificans enzyme can only carry out the synthetic reaction. The mechanism of inhibition of its ATP hydrolytic activity involves a zeta inhibitor protein, which binds to the catalytic F1-domain of the enzyme. The complex that has been crystallized, and the crystals themselves, contain the nine core proteins of the complete F-ATPase complex plus the zeta inhibitor protein. The formation of crystals depends upon the presence of bound bacterial cardiolipin and phospholipid molecules; when they were removed, the complex failed to crystallize. The experiments open the way to an atomic structure of an F-ATPase complex.
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