4B0Z

Crystal structure of S. pombe Rpn12

Summary for 4B0Z

• Entry DOI: 10.2210/pdb4b0z/pdb
• Descriptor: 26S PROTEASOME REGULATORY SUBUNIT RPN12, NITRATE ION, MONOTHIOGLYCEROL, ... (5 entities in total)
• Functional Keywords: protein binding, proteasome ubitquitin
• Biological source: SCHIZOSACCHAROMYCES POMBE
• Total number of polymer chains: 2
• Total formula weight: 53192.55

Authors

Boehringer, J.,Riedinger, C.,Paraskevopoulos, K.,Johnson, E.O.D.,Lowe, E.D.,Khoudian, C.,Smith, D.,Noble, M.E.M.,Gordon, C.,Endicott, J.A. (deposition date: 2012-07-06, release date: 2012-09-12, Last modification date: 2024-11-20)

Primary citation

Boehringer, J.,Riedinger, C.,Paraskevopoulos, K.,Johnson, E.O.D.,Lowe, E.D.,Khoudian, C.,Smith, D.,Noble, M.E.M.,Gordon, C.,Endicott, J.A.
Structural and Functional Characterisation of Rpn12 Identifies Residues Required for Rpn10 Proteasome Incorporation.
Biochem.J., 448:55-, 2012

PubMed Abstract: The ubiquitin-proteasome system targets selected proteins for degradation by the 26S proteasome. Rpn12 is an essential component of the 19S regulatory particle and plays a role in recruiting the extrinsic ubiquitin receptor Rpn10. In the present paper we report the crystal structure of Rpn12, a proteasomal PCI-domain-containing protein. The structure helps to define a core structural motif for the PCI domain and identifies potential sites through which Rpn12 might form protein-protein interactions. We demonstrate that mutating residues at one of these sites impairs Rpn12 binding to Rpn10 in vitro and reduces Rpn10 incorporation into proteasomes in vivo.

PubMed: 22906049
DOI: 10.1042/BJ20120542

Experimental method

X-RAY DIFFRACTION (1.585 Å)