ArticleProceedings of the National Academy of Sciences of the United States of America2008
Crystal structure of bovine mitochondrial factor B at 0.96-A resolution.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed, 18 citations in OpenAlex.
- Elucidating arsenic-bound proteins in the protein data bank: data mining and amino acid cross-validation through Raman spectroscopy.RSC advances · 2023Article
- The Mitochondrial Permeability Transition Pore: Channel Formation by F-ATP Synthase, Integration in Signal Transduction, and Role in Pathophysiology.Physiological reviews · 2015Review
- From ATP to PTP and Back: A Dual Function for the Mitochondrial ATP Synthase.Circulation research · 2015Review
- The oligomycin-sensitivity conferring protein of mitochondrial ATP synthase: emerging new roles in mitochondrial pathophysiology.International journal of molecular sciences · 2014Article
- Coupling factor B affects the morphology of mitochondria.Journal of bioenergetics and biomembranes · 2010Article
- Recent advances in structure-functional studies of mitochondrial factor B.Journal of bioenergetics and biomembranes · 2009Review
- Mitochondrial matters of the heart: a plethora of regulatory modes to maintain function for a long lifetime.Journal of bioenergetics and biomembranes · 2009Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Coupling factor B (FB) is a mitochondrial inner membrane polypeptide that facilitates the energy-driven catalysis of ATP synthesis in animal mitochondria by blocking a proton leak across the membrane. Here, we report the crystal structure of the bovine mitochondrial FB mutant with Gly-3-Glu substitution determined at a resolution of 0.96 A and that of the WT polypeptide at a resolution of 2.9 A. The structure reveals an oblong, oval-shaped molecule with a unique globular N-terminal domain that is proposed to be the membrane anchor domain and the capping region to the C-terminal leucine-rich repeats domain. A short N-terminal alpha-helix, which extends away from the molecule's body, is suggestive of functioning as an anchor for FB to the matrix side of the mitochondrial inner membrane. Identification of a bound Mg(2+) ion reveals that FB is a metalloprotein. We also report the cocrystal structures of FB bound with phenylarsine oxide and Cd(2+), two known inhibitors of the FB coupling activity.
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