Structural changes linked to proton translocation by subunit c of the ATP synthase

被引:379
作者
Rastogi, VK [1 ]
Girvin, ME [1 ]
机构
[1] Yeshiva Univ Albert Einstein Coll Med, Dept Biochem, Bronx, NY 10461 USA
关键词
D O I
10.1038/46224
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
F1F0 ATP synthases use a transmembrane proton gradient to drive the synthesis of cellular ATP. The structure of the cytosolic F-1 portion of the enzyme and the basic mechanism of ATP hydrolysis by F-1 are now well established, but how proton translocation through the transmembrane F-0 portion drives these catalytic changes is less clear. Here we describe the structural changes in the proton-translocating F-0 subunit c that are induced by deprotonating the specific aspartic acid involved in proton transport. conformational changes between the protonated and deprotonated forms of subunit c provide the structural basis for an explicit mechanism to explain coupling of proton translocation by F-0 to the rotation of subunits within the core of F-1. Rotation of these subunits within F-1 causes the catalytic conformational changes in the active sites of F-1 that result in ATP synthesis.
引用
收藏
页码:263 / 268
页数:6
相关论文
共 50 条
  • [1] STRUCTURE AT 2.8-ANGSTROM RESOLUTION OF F1-ATPASE FROM BOVINE HEART-MITOCHONDRIA
    ABRAHAMS, JP
    LESLIE, AGW
    LUTTER, R
    WALKER, JE
    [J]. NATURE, 1994, 370 (6491) : 621 - 628
  • [2] ARIS JP, 1983, J BIOL CHEM, V258, P4599
  • [3] Proton-translocating carboxyl of subunit c of F1Fo H+-ATP synthase: The unique environment suggested by the pK(a) determined by H-1 NMR
    AssadiPorter, FM
    Fillingame, RH
    [J]. BIOCHEMISTRY, 1995, 34 (49) : 16186 - 16193
  • [4] Temperature dependence of H-1 chemical shifts in proteins
    Baxter, NJ
    Williamson, MP
    [J]. JOURNAL OF BIOMOLECULAR NMR, 1997, 9 (04) : 359 - 369
  • [5] The 2.8-Å structure of rat liver F1-ATPase:: Configuration of a critical intermediate in ATP synthesis/hydrolysis
    Bianchet, MA
    Hullihen, J
    Pedersen, PL
    Amzel, LM
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1998, 95 (19) : 11065 - 11070
  • [6] BIRKENHAGER R, 1995, EUR J BIOCHEM, V230, P58, DOI 10.1111/j.1432-1033.1995.0058i.x
  • [7] The ATP synthase - A splendid molecular machine
    Boyer, PD
    [J]. ANNUAL REVIEW OF BIOCHEMISTRY, 1997, 66 : 717 - 749
  • [8] Crystallography & NMR system:: A new software suite for macromolecular structure determination
    Brunger, AT
    Adams, PD
    Clore, GM
    DeLano, WL
    Gros, P
    Grosse-Kunstleve, RW
    Jiang, JS
    Kuszewski, J
    Nilges, M
    Pannu, NS
    Read, RJ
    Rice, LM
    Simonson, T
    Warren, GL
    [J]. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1998, 54 : 905 - 921
  • [9] Energy transduction in the sodium F-ATPase of Propionigenium modestum
    Dimroth, P
    Wang, HY
    Grabe, M
    Oster, G
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1999, 96 (09) : 4924 - 4929
  • [10] Structure of the subunit c oligomer in the F1F0 ATP synthase:: Model derived from solution structure of the monomer and cross-linking in the native enzyme
    Dmitriev, OY
    Jones, PC
    Fillingame, RH
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1999, 96 (14) : 7785 - 7790