1KPS

Structural Basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin conjugating enzyme Ubc9 and RanGAP1

Summary for 1KPS

• Entry DOI: 10.2210/pdb1kps/pdb
• Descriptor: Ubiquitin-like protein SUMO-1 conjugating enzyme, Ran-GTPase activating protein 1, SULFATE ION, ... (4 entities in total)
• Functional Keywords: sumo, ubiquitin, e2, conjugating enzyme, ligase, thioester, small ubiquitin-like modifier, ligase-protein transport complex, ligase/protein transport
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: P63279; Cytoplasm : P46061
• Total number of polymer chains: 4
• Total formula weight: 73851.32

Authors

Bernier-Villamor, V.,Sampson, D.A.,Matunis, M.J.,Lima, C.D. (deposition date: 2002-01-02, release date: 2002-02-13, Last modification date: 2024-11-20)

Primary citation

Bernier-Villamor, V.,Sampson, D.A.,Matunis, M.J.,Lima, C.D.
Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1.
Cell(Cambridge,Mass.), 108:345-356, 2002

PubMed Abstract: 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.

PubMed: 11853669
DOI: 10.1016/S0092-8674(02)00630-X

Experimental method

X-RAY DIFFRACTION (2.5 Å)