2X5N

Crystal Structure of the SpRpn10 VWA domain

Summary for 2X5N

• Entry DOI: 10.2210/pdb2x5n/pdb
• Descriptor: 26S PROTEASOME REGULATORY SUBUNIT RPN10, SULFATE ION (3 entities in total)
• Functional Keywords: nuclear protein, nucleus, ubiquitin, proteasome
• Biological source: SCHIZOSACCHAROMYCES POMBE (FISSION YEAST)
• Cellular location: Nucleus: O94444
• Total number of polymer chains: 1
• Total formula weight: 21652.63

Authors

Riedinger, C.,Boehringer, J.,Trempe, J.-F.,Lowe, E.D.,Brown, N.R.,Gehring, K.,Noble, M.E.M.,Gordon, C.,Endicott, J.A. (deposition date: 2010-02-10, release date: 2010-08-25, Last modification date: 2024-05-08)

Primary citation

Riedinger, C.,Boehringer, J.,Trempe, J.F.,Lowe, E.D.,Brown, N.R.,Gehring, K.,Noble, M.E.,Gordon, C.,Endicott, J.A.
The Structure of Rpn10 and its Interactions with Polyubiquitin Chains and the Proteasome Subunit Rpn12.
J.Biol.Chem., 285:33992-, 2010

PubMed Abstract: Schizosaccharomyces pombe Rpn10 (SpRpn10) is a proteasomal ubiquitin (Ub) receptor located within the 19 S regulatory particle where it binds to subunits of both the base and lid subparticles. We have solved the structure of full-length SpRpn10 by determining the crystal structure of the von Willebrand factor type A domain and characterizing the full-length protein by NMR. We demonstrate that the single Ub-interacting motif (UIM) of SpRpn10 forms a 1:1 complex with Lys(48)-linked diUb, which it binds selectively over monoUb and Lys(63)-linked diUb. We further show that the SpRpn10 UIM binds to SpRpn12, a subunit of the lid subparticle, with an affinity comparable with Lys(48)-linked diUb. This is the first observation of a UIM binding other than a Ub fold and suggests that SpRpn12 could modulate the activity of SpRpn10 as a proteasomal Ub receptor.

PubMed: 20739285
DOI: 10.1074/JBC.M110.134510

Experimental method

X-RAY DIFFRACTION (1.3 Å)