1kmk: Difference between revisions
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|PDB= 1kmk |SIZE=350|CAPTION= <scene name='initialview01'>1kmk</scene>, resolution 2.2Å | |PDB= 1kmk |SIZE=350|CAPTION= <scene name='initialview01'>1kmk</scene>, resolution 2.2Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CSE:SELENOCYSTEINE'>CSE</scene> and <scene name='pdbligand=PLP:PYRIDOXAL-5 | |LIGAND= <scene name='pdbligand=CSE:SELENOCYSTEINE'>CSE</scene> and <scene name='pdbligand=PLP:PYRIDOXAL-5'-PHOSPHATE'>PLP</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Selenocysteine_lyase Selenocysteine lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.16 4.4.1.16] | |ACTIVITY= [http://en.wikipedia.org/wiki/Selenocysteine_lyase Selenocysteine lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.16 4.4.1.16] | ||
|GENE= | |GENE= | ||
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[[Category: structural genomic]] | [[Category: structural genomic]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 12:30:32 2008'' | ||
Revision as of 10:30, 23 March 2008
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| 1kmk, resolution 2.2Å | |||||||||||||
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| Ligands: | CSE and PLP | ||||||||||||
| Activity: | Selenocysteine lyase, with EC number 4.4.1.16 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
E. coli NifS/CsdB protein at 2.20A with the cysteine perselenide intermediate (residue CSZ).
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
1KMK is a Single protein structure of sequence from Escherichia coli. 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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Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- 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 genomic
