2x5n
From Proteopedia
Crystal Structure of the SpRpn10 VWA domain
Structural highlights
Function[RPN10_SCHPO] Protects ubiquitin chains against dissambly by deubiquitinating enzymes thereby promoting protein degradation.[1] [2] Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedSchizosaccharomyces pombe Rpn10 (SpRpn10) is a proteasomal ubiquitin (Ub) receptor located within the 19S regulatory particle where it binds to subunits of both the base and lid sub-particles. We have solved the structure of full-length SpRpn10 by determining the crystal structure of the VWA domain and characterising the full-length protein by NMR. We demonstrate that the single Ub interacting motif (UIM) of SpRpn10 forms a 1:1 complex with K48-linked diUb, which it binds selectively over monoUb and K63-linked diUb. We further show that the SpRpn10 UIM binds to SpRpn12, a subunit of the lid sub-particle, with an affinity comparable to Lys48-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. The structure of RPN10 and its interactions with polyubiquitin chains and the proteasome subunit RPN12.,Riedinger C, Boehringer J, Trempe JF, Lowe ED, Brown NR, Gehring K, Noble ME, Gordon C, Endicott JA J Biol Chem. 2010 Aug 24. PMID:20739285[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Categories: Cbs 356 | Large Structures | Boehringer, J | Brown, N R | Endicott, J A | Gehring, K | Gordon, C | Lowe, E D | Noble, M E.M | Riedinger, C | Trempe, J F | Nuclear protein | Nucleus | Proteasome | Ubiquitin