2vfj
From Proteopedia
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|PDB= 2vfj |SIZE=350|CAPTION= <scene name='initialview01'>2vfj</scene>, resolution 3.2Å | |PDB= 2vfj |SIZE=350|CAPTION= <scene name='initialview01'>2vfj</scene>, resolution 3.2Å | ||
|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+C'>AC1</scene>, <scene name='pdbsite=AC2:So4+Binding+Site+For+Chain+D'>AC2</scene>, <scene name='pdbsite=AC3:So4+Binding+Site+For+Chain+C'>AC3</scene>, <scene name='pdbsite=AC4:So4+Binding+Site+For+Chain+D'>AC4</scene> and <scene name='pdbsite=AC5:Mg+Binding+Site+For+Chain+D'>AC5</scene> | |SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+C'>AC1</scene>, <scene name='pdbsite=AC2:So4+Binding+Site+For+Chain+D'>AC2</scene>, <scene name='pdbsite=AC3:So4+Binding+Site+For+Chain+C'>AC3</scene>, <scene name='pdbsite=AC4:So4+Binding+Site+For+Chain+D'>AC4</scene> and <scene name='pdbsite=AC5:Mg+Binding+Site+For+Chain+D'>AC5</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Ubiquitinyl_hydrolase_1 Ubiquitinyl hydrolase 1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.12 3.4.19.12] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitinyl_hydrolase_1 Ubiquitinyl hydrolase 1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.12 3.4.19.12] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vfj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vfj OCA], [http://www.ebi.ac.uk/pdbsum/2vfj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2vfj RCSB]</span> | ||
}} | }} | ||
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[[Category: Barford, D.]] | [[Category: Barford, D.]] | ||
[[Category: Komander, D.]] | [[Category: Komander, D.]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: SO4]] | ||
[[Category: apoptosis]] | [[Category: apoptosis]] | ||
[[Category: cysteine protease]] | [[Category: cysteine protease]] | ||
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[[Category: zinc-finger]] | [[Category: zinc-finger]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:11:34 2008'' |
Revision as of 02:11, 31 March 2008
| |||||||
| , resolution 3.2Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , and | ||||||
| Ligands: | , | ||||||
| Activity: | Ubiquitinyl hydrolase 1, with EC number 3.4.19.12 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF THE A20 OVARIAN TUMOUR (OTU) DOMAIN
Overview
The NF-kappaB (nuclear factor kappaB) regulator A20 antagonises IKK [IkappaB (inhibitor of kappaB) kinase] activation by modulating Lys63-linked polyubiquitination of cytokine-receptor-associated factors including TRAF2/6 (tumour-necrosis-factor-receptor-associated factor 2/6) and RIP1 (receptor-interacting protein 1). In the present paper we describe the crystal structure of the N-terminal OTU (ovarian tumour) deubiquitinase domain of A20, which differs from other deubiquitinases but shares the minimal catalytic core with otubain-2. Analysis of conserved surface regions allows prediction of ubiquitin-binding sites for the proximal and distal ubiquitin molecules. Structural and biochemical analysis suggests a novel architecture of the catalytic triad, which might be present in a subset of OTU domains including Cezanne and TRABID (TRAF-binding domain). Biochemical analysis shows a preference of the isolated A20 OTU domain for Lys48-linked tetraubiquitin in vitro suggesting that additional specificity factors might be required for the physiological function of A20 in cells.
About this Structure
2VFJ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of the A20 OTU domain and mechanistic insights into deubiquitination., Komander D, Barford D, Biochem J. 2008 Jan 1;409(1):77-85. PMID:17961127
Page seeded by OCA on Mon Mar 31 05:11:34 2008
Categories: Homo sapiens | Single protein | Ubiquitinyl hydrolase 1 | Barford, D. | Komander, D. | Apoptosis | Cysteine protease | Cytokine signalling | Cytoplasm | Deubiquitinating enzyme | Dna-binding | Hydrolase | Lys63- linked | Metal-binding | Nf-kb | Nucleus | Otu | Ovarian tumour | Phosphorylation | Polymorphism | Protease | Thiol protease | Ubiquitin | Ubl conjugation pathway | Zinc | Zinc-finger
