1z7l

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[[Image:1z7l.gif|left|200px]]
[[Image:1z7l.gif|left|200px]]
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{{Structure
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|PDB= 1z7l |SIZE=350|CAPTION= <scene name='initialview01'>1z7l</scene>, resolution 2.80&Aring;
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The line below this paragraph, containing "STRUCTURE_1z7l", creates the "Structure Box" on the page.
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|SITE=
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|GENE= Ube1x, Uba1, Ube1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
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{{STRUCTURE_1z7l| PDB=1z7l | SCENE= }}
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|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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'''Crystal structure of fragment of mouse ubiquitin-activating enzyme'''
'''Crystal structure of fragment of mouse ubiquitin-activating enzyme'''
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[[Category: Filipek, R.]]
[[Category: Filipek, R.]]
[[Category: Szczepanowski, R H.]]
[[Category: Szczepanowski, R H.]]
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[[Category: scch]]
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[[Category: Scch]]
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[[Category: second catalytic cysteine half-domain]]
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[[Category: Second catalytic cysteine half-domain]]
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[[Category: ubiquitin-activating enzyme]]
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[[Category: Ubiquitin-activating enzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:16:40 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:31:15 2008''
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Revision as of 14:16, 3 May 2008

Template:STRUCTURE 1z7l

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 Page seeded by OCA on Sat May 3 17:16:40 2008

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