Molecular Basis for Bre5 Cofactor Recognition by the Ubp3 Deubiquitylating Enzyme.
From: The Wistar Institute University of Pennsylvania, Philadelphia, PA 19104, USA.
Journal of molecular biology
- Publish Date: Sep 2007
- ISSN: 0022-2836
- Volume: 372
- Issue: 1
- Pages: 194-204
- Medium: Print
- Language: English
- Citation (JAMA): Li Keqin, Ossareh-Nazari Batool, Liu Xin, et al. Molecular Basis for Bre5 Cofactor Recognition by the Ubp3 Deubiquitylating Enzyme.. J. Mol. Biol. Sep 2007;372:194-204
Abstract
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.
Mesh Headings (Keywords): Amino Acid Sequence, Binding Sites, Carrier Proteins, Coenzymes, Endopeptidases, Models, Molecular, Molecular Sequence Data, Mutagenesis, Site-Directed, Protein Binding, Protein Processing, Post-Translational, Protein Structure, Tertiary, Saccharomyces cerevisiae Proteins, Sequence Homology, Amino Acid, Ubiquitin
Check for Full Text / PubMed Unique Identifier (PMID): 17632125
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