Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1.
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.
Mesh Terms:
Amino Acid Sequence, Animals, Binding Sites, GTPase-Activating Proteins, Humans, Ligases, Models, Molecular, Molecular Sequence Data, Mutagenesis, Site-Directed, Protein Conformation, SUMO-1 Protein, Sequence Alignment, Structure-Activity Relationship, Substrate Specificity, Ubiquitin-Conjugating Enzymes
Amino Acid Sequence, Animals, Binding Sites, GTPase-Activating Proteins, Humans, Ligases, Models, Molecular, Molecular Sequence Data, Mutagenesis, Site-Directed, Protein Conformation, SUMO-1 Protein, Sequence Alignment, Structure-Activity Relationship, Substrate Specificity, Ubiquitin-Conjugating Enzymes
Cell
Date: Feb. 08, 2002
PubMed ID: 11853669
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