Skip to main content
. 2009 Apr 24;284(17):11336–11345. doi: 10.1074/jbc.M900374200

FIGURE 1.

FIGURE 1.

The βDELSEED-loop. A, interaction of the βTP and βE subunits with theγ subunit.β subunits are shown in yellow andγ in blue. The DELSEED-loop (shown in orange, with the DELSEED motif itself in green)of βTP interacts with the C-terminal helixγ and the short helix that runs nearly perpendicular to the rotation axis. The DELSEED-loop of βE makes contact with the convex portion of γ, formed mainly by the N-terminal helix. A nucleotide molecule (shown in stick representation) occupies the catalytic site of βTP, and the subunit is in the closed conformation. The catalytic site on βE is empty, and the subunit is in the open conformation. This figure is based on Protein Data Bank file 1e79 (32). B, deletions in the βDELSEED-loop. The loop was “mutated” in silico to represent the PS3 ATP synthase. The 3–4-residue segments that are removed in the deletion mutants are color-coded as follows: 380LQDI383, pink; 384IAIL387, green; 388GMDE391, yellow; 392LSD394, cyan; 395EDKL398, orange; 399VVHR402, blue. Residues that are the most involved in contacts with γ are labeled. All figures were generated using the program PyMOL (DeLano Scientific, San Carlos, CA).