1z7l
From Proteopedia
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|PDB= 1z7l |SIZE=350|CAPTION= <scene name='initialview01'>1z7l</scene>, resolution 2.80Å | |PDB= 1z7l |SIZE=350|CAPTION= <scene name='initialview01'>1z7l</scene>, resolution 2.80Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=TBR:HEXATANTALUM DODECABROMIDE'>TBR</scene> | + | |LIGAND= <scene name='pdbligand=TBR:HEXATANTALUM+DODECABROMIDE'>TBR</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= Ube1x, Uba1, Ube1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | |GENE= Ube1x, Uba1, Ube1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1z7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z7l OCA], [http://www.ebi.ac.uk/pdbsum/1z7l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1z7l RCSB]</span> | ||
}} | }} | ||
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[[Category: Filipek, R.]] | [[Category: Filipek, R.]] | ||
[[Category: Szczepanowski, R H.]] | [[Category: Szczepanowski, R H.]] | ||
| - | [[Category: TBR]] | ||
[[Category: scch]] | [[Category: scch]] | ||
[[Category: second catalytic cysteine half-domain]] | [[Category: second catalytic cysteine half-domain]] | ||
[[Category: ubiquitin-activating enzyme]] | [[Category: ubiquitin-activating enzyme]] | ||
| - | ''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 01:31:15 2008'' |
Revision as of 22:31, 30 March 2008
| |||||||
| , resolution 2.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | Ube1x, Uba1, Ube1 (Mus musculus) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of fragment of mouse ubiquitin-activating enzyme
Overview
Protein ubiquitination requires the sequential activity of three enzymes: a ubiquitin-activating enzyme (E1), a ubiquitin-conjugating enzyme (E2), and a ubiquitin-ligase (E3). The ubiquitin-transfer machinery is hierarchically organized; for every ubiquitin-activating enzyme, there are several ubiquitin-conjugating enzymes, and most ubiquitin-conjugating enzymes can in turn interact with multiple ubiquitin ligases. Despite the central role of ubiquitin-activating enzyme in this cascade, a crystal structure of a ubiquitin-activating enzyme is not available. The enzyme is thought to consist of an adenylation domain, a catalytic cysteine domain, a four-helix bundle, and possibly, a ubiquitin-like domain. Its adenylation domain can be modeled because it is clearly homologous to the structurally known adenylation domains of the activating enzymes for the small ubiquitin-like modifier (SUMO) and for the protein encoded by the neuronal precursor cell-expressed, developmentally down-regulated gene 8 (NEDD8). Low sequence similarity and vastly different domain lengths make modeling difficult for the catalytic cysteine domain that results from the juxtaposition of two catalytic cysteine half-domains. Here, we present a biochemical and crystallographic characterization of the two half-domains and the crystal structure of the larger, second catalytic cysteine half-domain of mouse ubiquitin-activating enzyme. We show that the domain is organized around a conserved folding motif that is also present in the NEDD8- and SUMO-activating enzymes, and we propose a tentative model for full-length ubiquitin-activating enzyme.
About this Structure
1Z7L is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Crystal structure of a fragment of mouse ubiquitin-activating enzyme., Szczepanowski RH, Filipek R, Bochtler M, J Biol Chem. 2005 Jun 10;280(23):22006-11. Epub 2005 Mar 16. PMID:15774460
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