Premium
Structure of a central stalk subunit F of prokaryotic V‐type ATPase/synthase from Thermus thermophilus
Author(s) -
Makyio Hisayoshi,
Iino Ryota,
Ikeda Chiyo,
Imamura Hiromi,
Tamakoshi Masatada,
Iwata Momi,
Stock Daniela,
Bernal Ricardo A,
Carpenter Elisabeth P,
Yoshida Masasuke,
Yokoyama Ken,
Iwata So
Publication year - 2005
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1038/sj.emboj.7600859
Subject(s) - thermus thermophilus , biology , protein subunit , atp synthase , stalk , atpase , thermus , biochemistry , enzyme , microbiology and biotechnology , escherichia coli , thermophile , gene , horticulture
The crystal structure of subunit F of vacuole‐type ATPase/synthase (prokaryotic V‐ATPase) was determined to of 2.2 Å resolution. The subunit reveals unexpected structural similarity to the response regulator proteins that include the Escherichia coli chemotaxis response regulator CheY. The structure was successfully placed into the low‐resolution EM structure of the prokaryotic holo‐V‐ATPase at a location indicated by the results of crosslinking experiments. The crystal structure, together with the single‐molecule analysis using fluorescence resonance energy transfer, showed that the subunit F exhibits two conformations, a ‘retracted’ form in the absence and an ‘extended’ form in the presence of ATP. Our results postulated that the subunit F is a regulatory subunit in the V‐ATPase.