Figure 1.
Figure 1 Close-ups of Sly1p−Sed5p interactions. (A) Stereo
diagram of the experimental electron density map of the
Sly1p−Sed5p complex. The region shows the conserved Sly1p
hydrophobic pocket (residues Leu137, Leu140, Ala141, Ile153 and
Val156) that accommodates the Sed5p key residue Phe10. The map
is contoured at 0.8 .
(B) Hydrogen bond network at the interface of Sly1p and Sed5p.
Residues 1−9 of Sed5p are shown as a ball-and-stick model in
yellow; residues 131−134, 138 and 156−160 of Sly1p are shown
in grey. Oxygen and nitrogen atoms are shown in red and blue,
respectively. Hydrogen bonds are indicated as dashed lines. Note
that the region comprising residues 10−21 of Sed5p is involved
in hydrophobic interactions only. (C) Superposition of domain I
of Sly1p in complex with Sed5p with the corresponding region in
s-Sec1 including a helical segment from a neighbouring molecule
forming a crystal contact (pdb code 1FVH). The r.m.s.d. for the
fragments shown is 1.34 Å within 127 residues (35
identical). The peptide backbones are shown as C[ ]-traces.
The colouring scheme is as follows: Sly1p, yellow; Sed5p, red;
s-Sec1 domain I, white; and s-Sec1 residues 321−332, mimicking
the Sed5p helical interaction, blue. N- and C-termini are
indicated.
.
(B) Hydrogen bond network at the interface of Sly1p and Sed5p.
Residues 1−9 of Sed5p are shown as a ball-and-stick model in
yellow; residues 131−134, 138 and 156−160 of Sly1p are shown
in grey. Oxygen and nitrogen atoms are shown in red and blue,
respectively. Hydrogen bonds are indicated as dashed lines. Note
that the region comprising residues 10−21 of Sed5p is involved
in hydrophobic interactions only. (C) Superposition of domain I
of Sly1p in complex with Sed5p with the corresponding region in
s-Sec1 including a helical segment from a neighbouring molecule
forming a crystal contact (pdb code 1FVH). The r.m.s.d. for the
fragments shown is 1.34 Å within 127 residues (35
identical). The peptide backbones are shown as C[ 
]-traces.
The colouring scheme is as follows: Sly1p, yellow; Sed5p, red;
s-Sec1 domain I, white; and s-Sec1 residues 321−332, mimicking
the Sed5p helical interaction, blue. N- and C-termini are
indicated.