Ontology highlight
ABSTRACT:
SUBMITTER: Yagi H
PROVIDER: S-EPMC2040882 | biostudies-literature | 2007 Jul
REPOSITORIES: biostudies-literature
Yagi Hiromasa H Kajiwara Nobumoto N Tanaka Hideaki H Tsukihara Tomitake T Kato-Yamada Yasuyuki Y Yoshida Masasuke M Akutsu Hideo H
Proceedings of the National Academy of Sciences of the United States of America 20070620 27
The epsilon 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 epsilon subunit from a thermophilic Bacillus PS3 at 1.9-A resolution. The C-terminal two alpha-helices were folded into a hairpin, sitting on the beta 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. ...[more]