1kps
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(New page: 200px<br /> <applet load="1kps" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kps, resolution 2.50Å" /> '''Structural Basis fo...)
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Revision as of 15:47, 12 November 2007
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Structural Basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin conjugating enzyme Ubc9 and RanGAP1
Overview
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.
About this Structure
1KPS is a Protein complex structure of sequences from Homo sapiens and Mus musculus with SO4 as ligand. Active as Ubiquitin--protein ligase, with EC number 6.3.2.19 Full crystallographic information is available from OCA.
Reference
Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1., Bernier-Villamor V, Sampson DA, Matunis MJ, Lima CD, Cell. 2002 Feb 8;108(3):345-56. PMID:11853669
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