Structural features of the γ subunit of the Escherichia coli F1 ATPase revealed by a 4.4-Å resolution map obtained by x-ray crystallography
Autor(en): | Hausrath, A.C. Grüber, G. Matthews, B.W. Capaldi, R.A. |
Stichwörter: | Proton-Translocating ATPases, EC 3.6.3.14; adenosine triphosphatase; bacterial protein; mitochondrial enzyme; protein subunit, alpha helix; article; crystallization; escherichia coli; liver mitochondrion; nonhuman; priority journal; protein structure; stoichiometry; structure analysis; X ray crystallography, Amino Acid Sequence; Animals; Cattle; Crystallography, X-Ray; Escherichia coli; Models, Molecular; Molecular Sequence Data; Peptide Mapping; Protein Conformation; Proton-Translocating ATPases; Rats, Bacteria (microorganisms); Escherichia coli | Erscheinungsdatum: | 1999 | Herausgeber: | National Academy of Sciences | Journal: | Proceedings of the National Academy of Sciences of the United States of America | Volumen: | 96 | Ausgabe: | 24 | Startseite: | 13697 | Seitenende: | 13702 | Zusammenfassung: | The F1 part of the F1F0 ATP synthase from Escherichia coli has been crystallized and its structure determined to 4.4-Å resolution by using molecular replacement based on the structure of the beef-heart mitochondrial enzyme. The bacterial F1 consists of five subunits with stoichiometry α3, β3, γ, δ, and ε. δ was removed before crystallization. In agreement with the structure of the beef-heart mitochondrial enzyme, although not that from rat liver, the present study suggests that the α and β subunits are arranged in a hexagonal barrel but depart from exact 3-fold symmetry. In the structures of both beef heart and rat-liver mitochondrial F1, less than half of the structure of the γ subunit was seen because of presumed disorder in the crystals. The present electron-density map includes a number of rod-shaped features which appear to correspond to additional α-helical regions within the γ subunit. These suggest that the γ subunit traverses the full length of the stalk that links the F1 and F0 parts and makes significant contacts with the c subunit ring of F0. |
ISSN: | 00278424 | DOI: | 10.1073/pnas.96.24.13697 | Externe URL: | https://www.scopus.com/inward/record.uri?eid=2-s2.0-0033598770&doi=10.1073%2fpnas.96.24.13697&partnerID=40&md5=9e38b2d4a531bf702fa562417b525475 |
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