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1kmk
From Proteopedia
| 1kmk, resolution 2.20Å () | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||||
| Non-Standard Residues: | |||||||||
| Activity: | Selenocysteine lyase, with EC number 4.4.1.16 | ||||||||
| Domains: | PRK09295, csdA | ||||||||
| Related: | 1jf9, 1kmj | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB, TOPSAN | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
E. coli NifS/CsdB protein at 2.20A with the cysteine perselenide intermediate (residue CSZ).
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.
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1KMK is a 1 chain structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
- Bernier-Villamor V, Sampson DA, Matunis MJ, Lima CD. Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1. Cell. 2002 Feb 8;108(3):345-56. PMID:11853669
Page seeded by OCA on Mon Feb 16 23:35:09 2009
Categories: Escherichia coli | Selenocysteine lyase | Burley, S K. | Lima, C D. | NYSGXRC, New York Structural GenomiX Research Consortium. | New york structural genomix research consortium | Nifs selenocysteine cysteine persulfide perselenide xray | Nysgxrc | Protein structure initiative | Psi | Structural genomic
