SMALL-ANGLE NEUTRON-SCATTERING FROM THE RECONSTITUTED TF1 OF H+-ATPASE FROM THERMOPHILIC BACTERIUM-PS3 WITH DEUTERATED SUBUNITS

被引:11
作者
ITO, Y
HARADA, M
OHTA, S
KAGAWA, Y
AONO, O
SCHEFER, J
SCHOENBORN, BP
机构
[1] UNIV TOKYO,INST SOLID STATE PHYS,MINATO KU,TOKYO 106,JAPAN
[2] JICHI MED SCH,DEPT BIOCHEM,MINAMI KAWACHI,TOCHIGI 32904,JAPAN
[3] JICHI MED SCH,DEPT PHYS,MINAMI KAWACHI,TOCHIGI 32904,JAPAN
[4] BROOKHAVEN NATL LAB,DEPT BIOL,UPTON,NY 11973
基金
美国国家科学基金会;
关键词
D O I
10.1016/S0022-2836(05)80191-3
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Subunits α, β and γ of adenosine triphosphatase (H+-ATPase) from the thermophilic bacterium PS3 (TF1) have been over-expressed in Escherichia coli. α and β subunits deuterated to the level of 90% were obtained by culturing E. coli in 2H2O medium. Both the subunits and the reconstituted αβγ complex, TF1, which contain the deuterated components in various combinations, were studied in solution by small-angle neutron scattering. The individual shapes of the subunits and their organization in the αβγ-TF1 complex were examined using the techniques of selective deuteration and contrast variation. The α and β subunits are well approximated as ellipsoids of revolution having minor semiaxes of 20·4(±0·4) and 20·0(±0·2) Å, and major semi-axes of 53·0(±1·4) and 55·8(±0·9) Å, respectively. In the TF1 complex, three β subunits are aligned to form an equilateral triangle, with their major axes tilted by 35° with respect to the 3-fold axis of the complex. The β-β distance is about 53 Å. Three α subunits are similarly arranged, positioned between the β subunits, and with their direction of tilt opposite to that of the β subunits. The centers of the α and β subunits lie in the same plane, forming a hexagon. Adjacent subunits overlap in this model, suggesting that they are not simple ellipsoids of revolution. © 1990 Academic Press Limited.
引用
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页码:289 / 302
页数:14
相关论文
共 29 条
  • [1] STRUCTURE OF THE MITOCHONDRIAL F1 ATPASE AT 9-A RESOLUTION
    AMZEL, LM
    MCKINNEY, M
    NARAYANAN, P
    PEDERSEN, PL
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES, 1982, 79 (19): : 5852 - 5856
  • [2] BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3
  • [3] NEW METHOD FOR DETERMINATION OF BIOLOGICAL QUARTERNARY STRUCTURE BY NEUTRON-SCATTERING
    ENGELMAN, DM
    MOORE, PB
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1972, 69 (08) : 1997 - &
  • [4] SMALL-ANGLE X-RAY-SCATTERING STUDY OF ADENOSINE-TRIPHOSPHATASE FROM THERMOPHILIC BACTERIUM PS3
    FURUNO, T
    IKEGAMI, A
    KIHARA, H
    YOSHIDA, M
    KAGAWA, Y
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 1983, 170 (01) : 137 - 153
  • [5] FUTAI M, 1983, MICROBIOL REV, V47, P258
  • [6] Guinier A., 1939, ANN PHYS-NEW YORK, V11, P161, DOI [DOI 10.1051/ANPHYS/193911120161, 10.1051/anphys/193911120161]
  • [7] HAMAMOTO T, 1985, ENZYMES BIOL MEMBR, V4, P149
  • [8] STUDY OF BIOLOGICAL STRUCTURES BY NEUTRON-SCATTERING FROM SOLUTION
    JACROT, B
    [J]. REPORTS ON PROGRESS IN PHYSICS, 1976, 39 (10) : 911 - 953
  • [9] ALPHA-3-BETA-3 COMPLEX OF THERMOPHILIC ATP SYNTHASE - CATALYSIS WITHOUT THE GAMMA-SUBUNIT
    KAGAWA, Y
    OHTA, S
    OTAWARAHAMAMOTO, Y
    [J]. FEBS LETTERS, 1989, 249 (01) : 67 - 69
  • [10] KAGAWA Y, 1984, BIOENERGETICS, P149