2qiy: Difference between revisions

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|SITE=  
|SITE=  
|LIGAND=  
|LIGAND=  
|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]  
|ACTIVITY= <span class='plainlinks'>[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] </span>
|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])
|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])
|DOMAIN=
|RELATEDENTRY=[[1zx2|1ZX2]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qiy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qiy OCA], [http://www.ebi.ac.uk/pdbsum/2qiy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2qiy RCSB]</span>
}}
}}


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[[Category: ubl conjugation pathway]]
[[Category: ubl conjugation pathway]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:26:17 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:49:47 2008''

Revision as of 04:49, 31 March 2008

File:2qiy.gif


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
Related: 1ZX2


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



yeast Deubiquitinase Ubp3 and Bre5 cofactor complex


OverviewOverview

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 StructureAbout this Structure

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

ReferenceReference

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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