Figure 1.
Fig. 1. Solution structures of the EEA1 FYVE domain. (A) The C
traces of
20 structures are shown that comprise EEA1 residues 1346 to 1410
in the lipid-free form, with the strands,
helix, hinge, membrane insertion loop, and zinc ions colored
green, magenta, cyan, brown, and orange, respectively. (B)
Ribbon diagram of the structure closest to the average. The 1, 2, 3, and 4 strands
and 1 helix
consist of residues 1370 to 1372, 1379 to 1381, 1387 to 1391,
1396 to 1400, and 1402 to 1408, respectively. The two zinc ions
(Zn1 and Zn2) are coordinated by eight cysteines whose side
chains are shown in yellow. (C) The C traces of
20 PtdIns(3)P-bound structures are depicted as in (A). The
PtdIns(3)P head group of the average structure is shown, with C
and P atoms in yellow and O atoms in red. (D) Superposition of
the PtdIns(3)P-bound and free structures, which are colored and
gray, respectively. The view has been rotated slightly to reveal
the structural differences.
The above figure is reprinted
by permission from the AAAs:
Science
(2001,
291,
1793-1796)
copyright 2001.
traces of
20 structures are shown that comprise EEA1 residues 1346 to 1410
in the lipid-free form, with the 
strands,
helix, hinge, membrane insertion loop, and zinc ions colored
green, magenta, cyan, brown, and orange, respectively. (B)
Ribbon diagram of the structure closest to the average. The