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Figure 1.
Figure 1. Structures of SENP2 deconjugation complexes with
RanGAP1–SUMO-1 and RanGAP1–SUMO-2. (a) Two nearly
orthogonal views of the human SENP2 catalytic domain in complex
with the C-terminal domain of RanGAP1 conjugated to either
SUMO-2 (left) or SUMO-1 (right), shown as ribbons. SENP2
catalytic residues are shown in bond representation, as is the
isopeptide bond between lysine and the SUMO diglycine motif. (b)
Stereo representation of the interaction between the SUMO-1
C-terminal tail (yellow), SENP2 (blue) and the consensus
residues of RanGAP1 (magenta), with interacting residues labeled
and shown in bond representation. Red dashed lines denote
putative hydrogen bonds. (c) Surface representation of SENP2 in
complex with the consensus residues of RanGAP1 conjugated to the
SUMO-1 diglycine motif. SUMO-1 C-terminal residues (yellow) and
RanGAP1 consensus motif (magenta) are shown as sticks. (d)
Stereo view of Ubc9 (SUMO E2, yellow) active site in complex
with RanGAP1–SUMO-1 (PDB 1Z5S)^29, depicted as in b. (e)
Simulated annealing omit map contoured at 1.2  ,
covering the isopeptide bond and selected active site residues
in the SENP2–RanGAP1–SUMO-1 structure. Graphics prepared
with PyMOL^41 (http://pymol.sourceforge.net).
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