2E5U

C-terminal domain of Epsilon subunit of F1F0-ATP synthase from the Thermophilic Bacillus PS3

Summary for 2E5U

• Entry DOI: 10.2210/pdb2e5u/pdb
• Related: 1AQT 1BSN 2E5T 2E5Y
• Descriptor: ATP synthase epsilon chain (1 entity in total)
• Functional Keywords: atp synthase, f1fo atp synthase, f1-atpase, epsilon subunit, atp, hydrolase
• Biological source: Bacillus sp. PS3
• Cellular location: Cell membrane; Peripheral membrane protein (By similarity): P07678
• Total number of polymer chains: 1
• Total formula weight: 4735.50

Authors

Yagi, H.,Akutsu, H. (deposition date: 2006-12-25, release date: 2007-07-10, Last modification date: 2024-05-29)

Primary citation

Yagi, H.,Kajiwara, N.,Tanaka, H.,Tsukihara, T.,Kato-Yamada, Y.,Yoshida, M.,Akutsu, H.
Structures of the thermophilic F1-ATPase {varepsilon} subunit suggesting ATP-regulated arm motion of its C-terminal domain in F1
Proc.Natl.Acad.Sci.Usa, 104:11233-11238, 2007

PubMed Abstract: 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. The E. coli epsilon subunit binds ATP in a similar manner, as judged on NMR. We also determined solution structures of the C-terminal domain of the PS3 epsilon 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 epsilon 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.

PubMed: 17581881
DOI: 10.1073/pnas.0701045104

Experimental method

SOLUTION NMR