1z7l: Difference between revisions
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[[Image:1z7l.gif|left|200px]] | [[Image:1z7l.gif|left|200px]] | ||
'''Crystal structure of fragment of mouse ubiquitin-activating enzyme''' | {{Structure | ||
|PDB= 1z7l |SIZE=350|CAPTION= <scene name='initialview01'>1z7l</scene>, resolution 2.80Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=TBR:HEXATANTALUM DODECABROMIDE'>TBR</scene> | |||
|ACTIVITY= | |||
|GENE= Ube1x, Uba1, Ube1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | |||
}} | |||
'''Crystal structure of fragment of mouse ubiquitin-activating enzyme''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1Z7L is a [ | 1Z7L is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z7L OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15774460 15774460] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: ubiquitin-activating enzyme]] | [[Category: ubiquitin-activating enzyme]] | ||
''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 15:32:08 2008'' | ||
Revision as of 13:32, 20 March 2008
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| 1z7l, resolution 2.80Å | |||||||||||||
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| Ligands: | TBR | ||||||||||||
| Gene: | Ube1x, Uba1, Ube1 (Mus musculus) | ||||||||||||
| 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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