TY - JOUR
T1 - Catalytic mechanism of F1-ATPase
AU - Weber, Joachim
AU - Senior, Alan E.
N1 - Funding Information:
Supported by NIH grant GM25349.
PY - 1997/3/28
Y1 - 1997/3/28
N2 - The structure of the core catalytic unit of ATP synthase, α3β3γ, has been determined by X-ray crystallography, revealing a roughly symmetrical arrangement of alternating α and β subunits around a central cavity in which helical portions of γ are found. A low-resolution structural model of F0, based on electron spectroscopic imaging, locates subunit a and the two copies of subunit b outside of a subunit c oligomer. The structures of individual subunits ε and c (largely) have been solved by NMR spectroscopy, but the oligomeric structure of c is still unknown. The structures of subunits a and δ remain undefined, that of b has not yet been defined but biochemical evidence indicates a credible model. Subunits γ, ε, b, and δ are at the interface between F1 and F0; γε complex forms one element of the stalk, interacting with c at the base and α and β at the top. The locations of b and δ are less clear. Elucidation of the structure F0, of the stalk, and of the entire F1F0 remains a challenging goal.
AB - The structure of the core catalytic unit of ATP synthase, α3β3γ, has been determined by X-ray crystallography, revealing a roughly symmetrical arrangement of alternating α and β subunits around a central cavity in which helical portions of γ are found. A low-resolution structural model of F0, based on electron spectroscopic imaging, locates subunit a and the two copies of subunit b outside of a subunit c oligomer. The structures of individual subunits ε and c (largely) have been solved by NMR spectroscopy, but the oligomeric structure of c is still unknown. The structures of subunits a and δ remain undefined, that of b has not yet been defined but biochemical evidence indicates a credible model. Subunits γ, ε, b, and δ are at the interface between F1 and F0; γε complex forms one element of the stalk, interacting with c at the base and α and β at the top. The locations of b and δ are less clear. Elucidation of the structure F0, of the stalk, and of the entire F1F0 remains a challenging goal.
KW - ATP synthase, FF
KW - Catalytic mechanism
KW - Oxidative phosphorylation
UR - http://www.scopus.com/inward/record.url?scp=0031588861&partnerID=8YFLogxK
U2 - 10.1016/S0005-2728(96)00121-1
DO - 10.1016/S0005-2728(96)00121-1
M3 - Review article
C2 - 9107315
AN - SCOPUS:0031588861
VL - 1319
SP - 19
EP - 58
JO - Biochimica et Biophysica Acta - Bioenergetics
JF - Biochimica et Biophysica Acta - Bioenergetics
SN - 0005-2728
IS - 1
ER -