2qiy

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[[Image:2qiy.gif|left|200px]]<br /><applet load="2qiy" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2qiy.gif|left|200px]]
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caption="2qiy, resolution 1.69&Aring;" />
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'''yeast Deubiquitinase Ubp3 and Bre5 cofactor complex'''<br />
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{{Structure
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|PDB= 2qiy |SIZE=350|CAPTION= <scene name='initialview01'>2qiy</scene>, resolution 1.69&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY= [http://en.wikipedia.org/wiki/Ubiquitin_thiolesterase Ubiquitin thiolesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.15 3.1.2.15]
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|GENE= BRE5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]), UBP3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
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}}
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'''yeast Deubiquitinase Ubp3 and Bre5 cofactor complex'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2QIY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Active as [http://en.wikipedia.org/wiki/Ubiquitin_thiolesterase Ubiquitin thiolesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.15 3.1.2.15] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QIY OCA].
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2QIY is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QIY OCA].
==Reference==
==Reference==
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Molecular basis for bre5 cofactor recognition by the ubp3 deubiquitylating enzyme., Li K, Ossareh-Nazari B, Liu X, Dargemont C, Marmorstein R, J Mol Biol. 2007 Sep 7;372(1):194-204. Epub 2007 Jun 27. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17632125 17632125]
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Molecular basis for bre5 cofactor recognition by the ubp3 deubiquitylating enzyme., Li K, Ossareh-Nazari B, Liu X, Dargemont C, Marmorstein R, J Mol Biol. 2007 Sep 7;372(1):194-204. Epub 2007 Jun 27. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17632125 17632125]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: phosphorylation]]
[[Category: phosphorylation]]
[[Category: protein-protein recognition]]
[[Category: protein-protein recognition]]
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[[Category: rna-binding ]]
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[[Category: rna-binding]]
[[Category: signaling protein/hydrolase complex]]
[[Category: signaling protein/hydrolase complex]]
[[Category: thiol protease]]
[[Category: thiol protease]]
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[[Category: ubl conjugation pathway]]
[[Category: ubl conjugation pathway]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:39:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:26:17 2008''

Revision as of 16:26, 20 March 2008


PDB ID 2qiy

Drag the structure with the mouse to rotate
, resolution 1.69Å
Gene: BRE5 (Saccharomyces cerevisiae), UBP3 (Saccharomyces cerevisiae)
Activity: Ubiquitin thiolesterase, with EC number 3.1.2.15
Coordinates: save as pdb, mmCIF, xml



yeast Deubiquitinase Ubp3 and Bre5 cofactor complex


Overview

Yeast Ubp3 and its co-factor Bre5 form a deubiquitylation complex to regulate protein transport between the endoplasmic reticulum and Golgi compartments of the cell. A novel N-terminal domain of the Ubp3 catalytic subunit forms a complex with the NTF2-like domain of the Bre5 regulatory subunit. Here, we report the X-ray crystal structure of an Ubp3-Bre5 complex and show that it forms a symmetric hetero-tetrameric complex in which the Bre5 NTF2-like domain dimer interacts with two L-shaped beta-strand-turn-alpha-helix motifs of Ubp3. The Ubp3 N-terminal domain binds within a hydrophobic cavity on the surface of the Bre5 NTF2-like domain subunit with conserved residues within both proteins interacting predominantly through antiparallel beta-sheet hydrogen bonds and van der Waals contacts. Structure-based mutagenesis and functional studies confirm the significance of the observed interactions for Ubp3-Bre5 association in vitro and Ubp3 function in vivo. Comparison of the structure to other protein complexes with NTF2-like domains shows that the Ubp3-Bre5 interface is novel. Together, these studies provide new insights into Ubp3 recognition by Bre5 and into protein recognition by NTF2-like domains.

About this Structure

2QIY is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Molecular basis for bre5 cofactor recognition by the ubp3 deubiquitylating enzyme., Li K, Ossareh-Nazari B, Liu X, Dargemont C, Marmorstein R, J Mol Biol. 2007 Sep 7;372(1):194-204. Epub 2007 Jun 27. PMID:17632125

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