2DZN

Crystal structure analysis of yeast Nas6p complexed with the proteasome subunit, rpt3

Summary for 2DZN

• Entry DOI: 10.2210/pdb2dzn/pdb
• Related: 2DZO
• Descriptor: Probable 26S proteasome regulatory subunit p28, 26S protease regulatory subunit 6B homolog (3 entities in total)
• Functional Keywords: ankyrin repeats, a-helical domain, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, protein binding
• Biological source: Saccharomyces cerevisiae (baker's yeast); More
• Cellular location: Cytoplasm (Potential): P33298
• Total number of polymer chains: 6
• Total formula weight: 104570.41

Authors

Yokoyama, S.,Padmanabhan, B.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2006-09-29, release date: 2007-07-17, Last modification date: 2024-04-03)

Primary citation

Nakamura, Y.,Umehara, T.,Tanaka, A.,Horikoshi, M.,Padmanabhan, B.,Yokoyama, S.
Structural basis for the recognition between the regulatory particles Nas6 and Rpt3 of the yeast 26S proteasome
Biochem.Biophys.Res.Commun., 359:503-509, 2007

PubMed Abstract: The 26S proteasome-dependent protein degradation is an evolutionarily conserved process. The mammalian oncoprotein gankyrin, which associates with S6 of the proteasome, facilitates the degradation of pRb, and thus possibly acts as a bridging factor between the proteasome and its substrates. However, the mechanism of the proteasome-dependent protein degradation in yeast is poorly understood. Here, we report the tertiary structure of the complex between Nas6 and a C-terminal domain of Rpt3, which are the yeast orthologues of gankyrin and S6, respectively. The concave region of Nas6 bound to the alpha-helical domain of Rpt3. The stable interaction between Nas6 and Rpt3 was mediated by intermolecular interactions composed of complementary charged patches. The recognition of Rpt3 by Nas6 in the crystal suggests that Nas6 is indeed a subunit of the 26S proteasome. These results provide a structural basis for the association between Nas6 and the heterohexameric ATPase ring of the proteasome through Rpt3.

PubMed: 17555716
DOI: 10.1016/j.bbrc.2007.05.138

Experimental method

X-RAY DIFFRACTION (2.2 Å)