Summary
PDB 1KPS deposited: 2002-01-02 modified: 2009-02-24
Title Structural Basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin conjugating enzyme Ubc9 and RanGAP1
Authors Bernier-Villamor, V., Lima, C.D., Matunis, M.J., Sampson, D.A.
Method X-RAY DIFFRACTION
Structure factors resolution 2.5 rfactor 0.223 rfree 0.3
DPI 0.92 theoretical min: 0.42
Citations

E2 enzymes catalyze attachment of ubiquitin and ubiquitin-like proteins to lysine residues directly or through E3-mediated reactions. The small ubiquitin-like modifier SUMO regulates nuclear transport, stress response, and signal transduction in eukaryotes and is essential for cell-cycle progression in yeast. In contrast to most ubiquitin conjugation, the SUMO E2 enzyme Ubc9 is sufficient for substrate recognition and lysine modification of known SUMO targets. Crystallographic analysis of a complex between mammalian Ubc9 and a C-terminal domain of RanGAP1 at 2.5 A reveals structural determinants for recognition of consensus SUMO modification sequences found within SUMO-conjugated proteins. Structure-based mutagenesis and biochemical analysis of Ubc9 and RanGAP1 reveal distinct motifs required for substrate binding and SUMO modification of p53, IkappaBalpha, and RanGAP1.

Cell(Cambridge,Mass.) 2002 Feb; 108(3):345-356 doi:10.1016/S0092-8674(02)00630-X

Cross References
Database source Identifier Description
PubMed 11853669 CELLB5
Biomolecule Structure Assembly Serial Assembly Type Conformational State Chains Ligands Atoms
1KPS/1 1KPS 1 dimer 0 2 2 2589
1KPS/2 1KPS 2 dimer 0 2 2 2533