1z7l
From Proteopedia
(New page: 200px<br /><applet load="1z7l" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z7l, resolution 2.80Å" /> '''Crystal structure of...) |
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| - | [[Image:1z7l.gif|left|200px]]<br /><applet load="1z7l" size=" | + | [[Image:1z7l.gif|left|200px]]<br /><applet load="1z7l" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1z7l, resolution 2.80Å" /> | caption="1z7l, resolution 2.80Å" /> | ||
'''Crystal structure of fragment of mouse ubiquitin-activating enzyme'''<br /> | '''Crystal structure of fragment of mouse ubiquitin-activating enzyme'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Protein ubiquitination requires the sequential activity of three enzymes: | + | 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== | ==About this Structure== | ||
| - | 1Z7L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with TBR as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1Z7L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=TBR:'>TBR</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z7L OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bochtler, M.]] | [[Category: Bochtler, M.]] | ||
[[Category: Filipek, R.]] | [[Category: Filipek, R.]] | ||
| - | [[Category: Szczepanowski, R | + | [[Category: Szczepanowski, R H.]] |
[[Category: TBR]] | [[Category: TBR]] | ||
[[Category: scch]] | [[Category: scch]] | ||
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[[Category: ubiquitin-activating enzyme]] | [[Category: ubiquitin-activating enzyme]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:12:53 2008'' |
Revision as of 14:12, 21 February 2008
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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 with as ligand. 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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