| Autor: |
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 |
| Předmět: |
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| Zdroj: |
EMBO Journal; 11/16/2005, Vol. 24 Issue 22, p3974-3983, 10p |
| Abstrakt: |
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. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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