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 13:30, 23 March 2008
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| , resolution 2.2Å | |||||||
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| Ligands: | and | ||||||
| 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).
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. 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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- 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