2YMA

X-ray structure of the Yos9 dimerization domain

Summary for 2YMA

• Entry DOI: 10.2210/pdb2yma/pdb
• Descriptor: PROTEIN OS-9 HOMOLOG (2 entities in total)
• Functional Keywords: carbohydrate binding protein, quality control, endoplasmic reticulum-associated protein degradation, hrd complex, misfolded proteins, endoplasmic reticulum
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• Cellular location: Endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side: Q99220
• Total number of polymer chains: 2
• Total formula weight: 36516.73

Authors

Hanna, J.,Schuetz, A.,Zimmermann, F.,Behlke, J.,Sommer, T.,Heinemann, U. (deposition date: 2011-06-07, release date: 2012-01-25, Last modification date: 2024-05-01)

Primary citation

Hanna, J.,Schutz, A.,Zimmermann, F.,Behlke, J.,Sommer, T.,Heinemann, U.
Structural and Biochemical Basis of Yos9 Protein Dimerization and Possible Contribution to Self-Association of 3-Hydroxy-3-Methylglutaryl-Coenzyme a Reductase Degradation Ubiquitin-Ligase Complex.
J.Biol.Chem., 287:8633-, 2012

PubMed Abstract: In yeast, the membrane-bound HMG-CoA reductase degradation (HRD) ubiquitin-ligase complex is a key player of the ER-associated protein degradation pathway that targets misfolded proteins for proteolysis. Yos9, a component of the luminal submodule of the ligase, scans proteins for specific oligosaccharide modifications, which constitute a critical determinant of the degradation signal. Here, we report the crystal structure of the Yos9 domain that was previously suggested to confer binding to Hrd3, another component of the HRD complex. We observe an αβ-roll domain architecture and a dimeric assembly which are confirmed by analytical ultracentrifugation of both the crystallized domain and full-length Yos9. Our binding studies indicate that, instead of this domain, the N-terminal part of Yos9 including the mannose 6-phosphate receptor homology domain mediates the association with Hrd3 in vitro. Our results support the model of a dimeric state of the HRD complex and provide first-time evidence of self-association on its luminal side.

PubMed: 22262864
DOI: 10.1074/JBC.M111.317644

Experimental method

X-RAY DIFFRACTION (2.545 Å)