Structures of the thermophilic F1-ATPase ε subunit suggesting ATP-regulated arm motion of its C-terminal domain in F1
The ε subunit of bacterial and chloroplast F o F 1 -ATP synthases modulates their ATP hydrolysis activity. Here, we report the crystal structure of the ATP-bound ε subunit from a thermophilic Bacillus PS3 at 1.9-Å resolution. The C-terminal two α-helices were folded into a hairpin, sitting on the β...
Saved in:
Published in | Proceedings of the National Academy of Sciences - PNAS Vol. 104; no. 27; pp. 11233 - 11238 |
---|---|
Main Authors | , , , , , , |
Format | Journal Article |
Language | English |
Published |
United States
National Acad Sciences
03.07.2007
National Academy of Sciences |
Subjects | |
Online Access | Get full text |
Cover
Loading…
Summary: | The ε subunit of bacterial and chloroplast F o F 1 -ATP synthases modulates their ATP hydrolysis activity. Here, we report the crystal structure of the ATP-bound ε subunit from a thermophilic Bacillus PS3 at 1.9-Å resolution. The C-terminal two α-helices were folded into a hairpin, sitting on the β sandwich structure, as reported for Escherichia coli . A previously undescribed ATP binding motif, I(L)DXXRA, recognizes ATP together with three arginine and one glutamate residues. The E. coli ε subunit binds ATP in a similar manner, as judged on NMR. We also determined solution structures of the C-terminal domain of the PS3 ε subunit and relaxation parameters of the whole molecule by NMR. The two helices fold into a hairpin in the presence of ATP but extend in the absence of ATP. The latter structure has more helical regions and is much more flexible than the former. These results suggest that the ε C-terminal domain can undergo an arm-like motion in response to an ATP concentration change and thereby contribute to regulation of F o F 1 -ATP synthase. ATP hydrolysis ATP-binding motif ATPase regulation ATP synthase F1 rotation |
---|---|
Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Author contributions: H.Y., M.Y., and H.A. designed research; H.Y., N.K., H.T., T.T., and H.A. performed research; Y.K.-Y. contributed new reagents/analytic tools; H.Y., N.K., H.T., T.T., and H.A. analyzed data; and H.Y., N.K., H.T., M.Y., and H.A. wrote the paper. Edited by Paul D. Boyer, University of California, Los Angeles, CA, and approved May 23, 2007 |
ISSN: | 0027-8424 1091-6490 |
DOI: | 10.1073/pnas.0701045104 |