Structural insights into the A(1) ATPase from the archaeon, Methanosarcina mazei Go1

Autor(en): Gruber, G
Svergun, DI
Coskun, U
Lemker, T
Koch, MHJ
Schagger, H
Muller, V
Stichwörter: Biochemistry & Molecular Biology; CELL-ENVELOPE VESICLES; ELECTRON-MICROSCOPY; F-1 ATPASE; GAMMA-SUBUNIT; HALOBACTERIUM-HALOBIUM; LOW-RESOLUTION STRUCTURE; SMALL-ANGLE-SCATTERING; SYNCHROTRON RADIATION; TRYPSIN DIGESTION; VACUOLAR ATPASE
Erscheinungsdatum: 2001
Herausgeber: AMER CHEMICAL SOC
Enthalten in: BIOCHEMISTRY
Band: 40
Ausgabe: 7
Startseite: 1890
Seitenende: 1896
Zusammenfassung: 
The low-resolution structure and overall dimensions of the A(3)B(3)CDF complex of the A(1) ATPase from Methanosarcina mazei Gol in solution is analyzed by synchrotron X-ray small-angle scattering. The radius of gyration and the maximum size of the complex are 5.03 /- 0.1 and 18.0 /- 0.1 nm, respectively. The low-resolution shape of the protein determined by two independent ab initio approaches has a knob-and-stalk-like feature. Its headpiece is approximately 9.4 nm long and 9.2 nm wide. The stalk, which is known to connect the headpiece to its membrane-bound A(o) part, is approximately 8.4 nm long. Limited tryptic digestion of the A(3)B(3)CDF complex was used to probe the topology of the smaller subunits (C-F). Trypsin was found to cleave subunit C most rapidly at three sites, Lys(20), LYs(21), and Arg(209), followed by subunit F. In the A(3)B(3)CDF complex, subunit D remained protected from proteolysis.
ISSN: 00062960
DOI: 10.1021/bi002195t

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