2qiy: Difference between revisions

Revision as of 13:07, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2qiy.png

Template:STRUCTURE 2qiy

yeast Deubiquitinase Ubp3 and Bre5 cofactor complexyeast Deubiquitinase Ubp3 and Bre5 cofactor complex

Template:ABSTRACT PUBMED 17632125

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

Structural basis for interaction between the Ubp3 deubiquitinating enzyme and its Bre5 cofactor., Li K, Zhao K, Ossareh-Nazari B, Da G, Dargemont C, Marmorstein R, J Biol Chem. 2005 Aug 12;280(32):29176-85. Epub 2005 Jun 13. PMID:15955808

Page seeded by OCA on Sun Jul 27 13:07:07 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:2qiy.gif|left|200px]]
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 {{STRUCTURE_2qiy|  PDB=2qiy  |  SCENE=  }}
-'''yeast Deubiquitinase Ubp3 and Bre5 cofactor complex'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_17632125}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17632125 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17632125}}
 ==About this Structure==
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 ==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:[http://www.ncbi.nlm.nih.gov/pubmed/17632125 17632125]
+Structural basis for interaction between the Ubp3 deubiquitinating enzyme and its Bre5 cofactor., Li K, Zhao K, Ossareh-Nazari B, Da G, Dargemont C, Marmorstein R, J Biol Chem. 2005 Aug 12;280(32):29176-85. Epub 2005 Jun 13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15955808 15955808]
 [[Category: Protein complex]]
 [[Category: Saccharomyces cerevisiae]]
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 [[Category: Thiol protease]]
 [[Category: Ubl conjugation pathway]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 15:02:07 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:07:07 2008''