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Figure 2.
Figure 2. Stereo views of the HslUV-NLVS inhibitor complex.
(a) View showing the hydrogen bonding interactions of the
inhibitor with HslV polypeptide backbone in the HslUV-NLVS
complex. Carbon atoms of HslV are green; carbon atoms of
inhibitor are gray; nitrogen atoms, blue; oxygen atoms, red;
sulfur atom, yellow. (b) Superposition of the substrate binding
clefts of HslUV-NLVS and the yeast proteasome with epoxomycin
(subunit K of PDB 1G65).[15.] Hydrogen bonds between protein and
inhibitor are the same as shown in part (a). Selected residues
are labeled with format "HslV#/proteasome#". Color scheme: HslV
of HslUV-NLVS complex, green; NLVS inhibitor atoms, cyan;
proteasome, red; epoxomycin inhibitor atoms, gold. (c) View
showing the inhibitor (semi-transparent CPK model) and the
binding pockets of HslUV. HslV protomer to which NLVS is
covalently attached is green; adjacent HslV protomer, yellow;
HslU, magenta; inhibitor, gray. Selected side chains are
included. Carbon atoms are the same color as corresponding
protomer; oxygen atoms, red; nitrogen atoms, blue; sulfur atoms,
cyan. (d) View showing the displacement of upper strand of
substrate binding cleft of uncomplexed HslV [9.] relative to
HslUV-NLVS; when lower segments of polypeptides are
superimposed, upper segment of uncomplexed HslV is displaced
 vert,
similar 3-4 Å from its position in the HslUV-NLVS complex.
For clarity, only selected peptide backbone and C^a atoms of the
proteins and "backbone" atoms of the inhibitor are included.
Color scheme: HslV of HslUV-NLVS complex, green; NLVS inhibitor
atoms, cyan; uncomplexed HslV, magenta. Superpositions were
computed with the program LSQMAN.[27.] The Figure was prepared
with MOLSCRIPT [28.] and RASTER3D. [26.]
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