1n87
Solution structure of the U-box of Prp19
|
OverviewOverview
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.
About this StructureAbout this Structure
1N87 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
Structural insights into the U-box, a domain associated with multi-ubiquitination., Ohi MD, Vander Kooi CW, Rosenberg JA, Chazin WJ, Gould KL, Nat Struct Biol. 2003 Apr;10(4):250-5. PMID:12627222
Page seeded by OCA on Tue Nov 20 22:02:21 2007