Journal
CURRENT OPINION IN STRUCTURAL BIOLOGY
Volume 33, Issue -, Pages 135-145Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2015.08.008
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Funding
- Medical Research Council [MC_U105674180] Funding Source: Medline
- MRC [MC_U105674180] Funding Source: UKRI
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The 1 MDa, 45-subunit proton-pumping NADH-ubiquinone oxidoreductase (complex I) is the largest complex of the mitochondrial electron transport chain. The molecular mechanism of complex I is central to the metabolism of cells, but has yet to be fully characterized. The last two years have seen steady progress towards this goal with the first atomic-resolution structure of the entire bacterial complex I, a 5 angstrom cryo-electron microscopy map of bovine mitochondrial complex I and a similar to 3.8 angstrom resolution X-ray crystallographic study of mitochondrial complex I from yeast Yarrowia lipotytica. In this review we will discuss what we have learned from these studies and what remains to be elucidated.
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