Conformational transmission in ATP synthase during catalysis: Search for large structural changes |
| |
Authors: | Masamitsu Futai Hiroshi Omote |
| |
Affiliation: | (1) Division of Biological Sciences, The Institute of Scientific and Industrial Research, Osaka University, Ibaraki, 567 Osaka, Japan |
| |
Abstract: | Escherichia coli ATP synthase has eight subunits and functions through transmission of conformational changes between subunits. Defective mutation at Gly-149 was suppressed by the second mutations at the outer surface of the subunit, indicating that the defect by the first mutation was suppressed by the second mutation through long range conformation transmission. Extensive mutant/pseudorevertant studies revealed that / and / subunits interactions are important for the energy coupling between catalysis and H+ translocation. In addition, long range interaction between amino and carboxyl terminal regions of the subunit has a critical role(s) for energy coupling. These results suggest that the dynamic conformation change and its transmission are essential for ATP synthase. |
| |
Keywords: | ATP synthase conformation transmission mutagenesis pseudorevertant rotational catalysis |
本文献已被 SpringerLink 等数据库收录! |