期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：2015
卷号：92
期号：22
页码：10379-10383
DOI：10.1073/pnas.1510577112
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：SignificanceMitochondrial complex I (proton-pumping NADH:ubiquinone oxidoreductase) is the largest respiratory chain enzyme. Mammalian complex I contains 45 subunits: the structures of the 14 "core" subunits (which are sufficient for catalysis and conserved from bacteria to humans) were described in the 5-[IMG]f1.gif" ALT="A" BORDER="0"> resolution structure of Bos taurus complex I, but only 14 supernumerary subunits could be located. Here, we exploit new structural information from the membrane domain of mammalian complex I to assign eight further supernumerary subunits. We locate two oxidatively-folded CHCH-domain subunits in the intermembrane space, and reveal a second LYR protein-acyl carrier protein module. Thus, we extend knowledge of how the supernumerary subunits are arranged around the core, and provide insights into their roles in biogenesis and regulation. Mitochondrial complex I (proton-pumping NADH:ubiquinone oxidoreductase) is an essential respiratory enzyme. Mammalian complex I contains 45 subunits: 14 conserved "core" subunits and 31 "supernumerary" subunits. The structure of Bos taurus complex I, determined to 5-[IMG]f1.gif" ALT="A" BORDER="0"> resolution by electron cryomicroscopy, described the structure of the mammalian core enzyme and allowed the assignment of 14 supernumerary subunits. Here, we describe the 6.8-[IMG]f1.gif" ALT="A" BORDER="0"> resolution X-ray crystallography structure of subcomplex I{beta
