1kmk: Difference between revisions
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[[Image:1kmk.gif|left|200px]] | [[Image:1kmk.gif|left|200px]] | ||
'''E. coli NifS/CsdB protein at 2.20A with the cysteine perselenide intermediate (residue CSZ).''' | {{Structure | ||
|PDB= 1kmk |SIZE=350|CAPTION= <scene name='initialview01'>1kmk</scene>, resolution 2.2Å | |||
|SITE= | |||
|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] | |||
|GENE= | |||
}} | |||
'''E. coli NifS/CsdB protein at 2.20A with the cysteine perselenide intermediate (residue CSZ).''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1KMK is a [ | 1KMK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KMK OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11853669 11853669] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Selenocysteine lyase]] | [[Category: Selenocysteine lyase]] | ||
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[[Category: protein structure initiative]] | [[Category: protein structure initiative]] | ||
[[Category: psi]] | [[Category: psi]] | ||
[[Category: structural | [[Category: structural genomic]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:19:25 2008'' | ||
Revision as of 10:19, 20 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
Page seeded by OCA on Thu Mar 20 12:19:25 2008
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