2BAY

Crystal structure of the Prp19 U-box dimer

Summary for 2BAY

• Entry DOI: 10.2210/pdb2bay/pdb
• Descriptor: Pre-mRNA splicing factor PRP19 (2 entities in total)
• Functional Keywords: prp19, u-box, ubiquitin ligase, e3 ligase, ligase
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Nucleus: P32523
• Total number of polymer chains: 6
• Total formula weight: 40366.28

Authors

Vander Kooi, C.W.,Ohi, M.D.,Rosenberg, J.A.,Oldham, M.L.,Newcomer, M.E.,Gould, K.L.,Chazin, W.J. (deposition date: 2005-10-15, release date: 2006-01-10, Last modification date: 2024-02-14)

Primary citation

Vander Kooi, C.W.,Ohi, M.D.,Rosenberg, J.A.,Oldham, M.L.,Newcomer, M.E.,Gould, K.L.,Chazin, W.J.
The Prp19 U-box Crystal Structure Suggests a Common Dimeric Architecture for a Class of Oligomeric E3 Ubiquitin Ligases.
Biochemistry, 45:121-130, 2006

PubMed Abstract: Prp19 is an essential splicing factor and a member of the U-box family of E3 ubiquitin ligases. Prp19 forms a tetramer via a central coiled-coil domain. Here, we show the U-box domain of Prp19 exists as a dimer within the context of the Prp19 tetramer. A high-resolution structure of the homodimeric state of the Prp19 U-box was determined by X-ray crystallography. Mutation of the U-box dimer interface abrogates U-box dimer formation and is lethal in vivo. The structure of the U-box dimer enables construction of a complete model of Prp19 providing insights into how the tetrameric protein functions as an E3 ligase. Finally, comparison of the Prp19 U-box homodimer with the heterodimeric complex of BRCA1/BARD1 RING-finger domains uncovers a common architecture for a family of oligomeric U-box and RING-finger E3 ubiquitin ligases, which has mechanistic implications for E3 ligase-mediated polyubiquitination and E4 polyubiquitin ligases.

PubMed: 16388587
DOI: 10.1021/bi051787e

Experimental method

X-RAY DIFFRACTION (1.5 Å)