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| - | [[Image:1z7l.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1z7l| PDB=1z7l | SCENE= }} | | {{STRUCTURE_1z7l| PDB=1z7l | SCENE= }} |
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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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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15774460}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15774460 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15774460}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[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 Sat May 3 17:16:40 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:15:30 2008'' |
Revision as of 12:15, 27 July 2008
Template:STRUCTURE 1z7l
Crystal structure of fragment of mouse ubiquitin-activating enzyme
Template:ABSTRACT PUBMED 15774460
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 Sun Jul 27 15:15:30 2008
