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2bay
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(New page: 200px<br /><applet load="2bay" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bay, resolution 1.50Å" /> '''Crystal structure of...)
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Revision as of 06:33, 21 November 2007
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Crystal structure of the Prp19 U-box dimer
Overview
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.
About this Structure
2BAY is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
The Prp19 U-box crystal structure suggests a common dimeric architecture for a class of oligomeric E3 ubiquitin ligases., Vander Kooi CW, Ohi MD, Rosenberg JA, Oldham ML, Newcomer ME, Gould KL, Chazin WJ, Biochemistry. 2006 Jan 10;45(1):121-30. PMID:16388587
Page seeded by OCA on Wed Nov 21 08:41:14 2007
