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EC Number
Crystallization (Commentary)
3.4.22.B71
recombinant chimeric mutant SENP2 C548S-loop1 in complex with SUMO2, X-ray diffraction structure determination and analysis at 2.15 A resolution
3.4.22.B71
Senp2 crystallization is performed at 4°C using sitting and hanging drop vapor diffusion methods. X-ray structures of Senp2 catalytic protease domain and of a covalent thiohemiacetal transition-state complex obtained between the Senp2 catalytic domain and SUMO-1 reveales details of the respective protease and substrate surfaces utilized in interactions between these two proteins. Comparative biochemical and structural analysis between Senp2 and the yeast SUMO protease Ulp1 reveales differential abilities to process SUMO-1, SUMO-2, and SUMO-3 in maturation and deconjugation reactions
3.4.22.B71
X-ray structures are determined for a catalytically inert SENP2 protease domain in complex with conjugated RanGAP1-SUMO-1 or RanGAP1-SUMO-2, or in complex with SUMO-2 or SUMO-3 precursors
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