1kmk
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E. coli NifS/CsdB protein at 2.20A with the cysteine perselenide intermediate (residue CSZ).
OverviewOverview
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 StructureAbout this Structure
1KMK is a Single protein structure of sequence from Escherichia coli with CSE and PLP as ligands. Active as Selenocysteine lyase, with EC number 4.4.1.16 Full crystallographic information is available from OCA.
ReferenceReference
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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- Escherichia coli
- Selenocysteine lyase
- Single protein
- Burley, S.K.
- Lima, C.D.
- NYSGXRC, New.York.Structural.GenomiX.Research.Consortium.
- CSE
- PLP
- New york structural genomix research consortium
- Nifs selenocysteine cysteine persulfide perselenide xray
- Nysgxrc
- Protein structure initiative
- Psi
- Structural genomics