Molecular architecture of Manduca sexta midgut V-1 ATPase visualized by electron microscopy

Autor(en): Radermacher, M
Ruiz, T
Harvey, WR
Wieczorek, H 
Gruber, G
Stichwörter: Biochemistry & Molecular Biology; BIOLOGICAL MACROMOLECULES; Biophysics; Cell Biology; electron microscopy; ESCHERICHIA-COLI; image processing; IMAGES; Manduca sexta; MEMBRANE; PARTICLES; PURIFICATION; SUBUNIT; TOBACCO HORNWORM MIDGUT; V-1 ATPase; VACUOLAR-TYPE ATPASE
Erscheinungsdatum: 1999
Herausgeber: ELSEVIER SCIENCE BV
Journal: FEBS LETTERS
Volumen: 453
Ausgabe: 3
Startseite: 383
Seitenende: 386
Zusammenfassung: 
The structure of the V-1 ATPase from the tobacco hornworm Manduca sexta has been determined from electron micrographs of isolated, negatively stained specimens. The resulting images clearly show a pseudohexagonal arrangement of six equal-sized protein densities, presumably representing the three copies each of subunits A and B, which comprise the headpiece of the enzyme. A seventh density could be observed either centrally or asymmetrically to the hexamer, The maximum diameter of the V-1 complex in the hexagonal projection is 13 nm with each of the six peripheral densities being 3-4 nm in diameter. (C) 1999 Federation of European Biochemical Societies.
ISSN: 00145793
DOI: 10.1016/S0014-5793(99)00739-5

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