1N87

Solution structure of the U-box of Prp19

Summary for 1N87

• Entry DOI: 10.2210/pdb1n87/pdb
• Descriptor: Pre-mRNA splicing factor PRP19 (1 entity in total)
• Functional Keywords: ubiquitin ligase, e3 ligase, u-box, ligase-cell cycle complex, ligase/cell cycle
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Nucleus: P32523
• Total number of polymer chains: 1
• Total formula weight: 6246.23

Authors

Chazin, W.J.,Ohi, M.D.,Vander Kooi, C.W. (deposition date: 2002-11-19, release date: 2003-04-15, Last modification date: 2024-05-22)

Primary citation

Ohi, M.D.,Vander Kooi, C.W.,Rosenberg, J.A.,Chazin, W.J.,Gould, K.L.
Structural insights into the U-box, a domain associated with multi-ubiquitination
Nat.Struct.Biol., 10:250-255, 2003

PubMed Abstract: The structure of the U-box in the essential Saccharomyces cerevisiae pre-mRNA splicing factor Prp19p has been determined by NMR. The conserved zinc-binding sites supporting the cross-brace arrangement in RING-finger domains are replaced by hydrogen-bonding networks in the U-box. These hydrogen-bonding networks are necessary for the structural stabilization and activity of the U-box. A conservative Val-->Ile point mutation in the Prp19p U-box domain leads to pre-mRNA splicing defects in vivo. NMR analysis of this mutant shows that the substitution disrupts structural integrity of the U-box domain. Furthermore, comparison of the Prp19p U-box domain with known RING-E2 complex structures demonstrates that both U-box and RING-fingers contain a conserved interaction surface. Mutagenesis of residues at this interface, while not perturbing the structure of the U-box, abrogates Prp19p function in vivo. These comparative structural and functional analyses imply that the U-box and its associated ubiquitin ligase activity are critical for Prp19p function in vivo.

PubMed: 12627222
DOI: 10.1038/nsb906

Experimental method

SOLUTION NMR