1ndd
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STRUCTURE OF NEDD8
OverviewOverview
The NEDD8/Rub1 class of ubiquitin-like proteins has been implicated in, progression of the cell cycle from G1 into S phase. These molecules, undergo a metabolism that parallels that of ubiquitin and involves, specific interactions with many different proteins. We report here the, crystal structure of recombinant human NEDD8 refined at 1.6-A resolution, to an R factor of 21.9%. As expected from the high sequence similarity, (57% identical), the NEDD8 structure closely resembles that reported, previously for ubiquitin. We also show that recombinant human NEDD8, protein is activated, albeit inefficiently, by the ubiquitin-activating, (E1) enzyme and that NEDD8 can be transferred from E1 to the ubiquitin, conjugating enzyme E2-25K. E2-25K adds NEDD8 to a polyubiquitin chain with, an efficiency similar to that of ubiquitin. A chimeric tetramer composed, of three ubiquitins and one histidine-tagged NEDD8 binds to the 26 S, proteasome with an affinity similar to that of tetraubiquitin. Seven, residues that differ from the corresponding residues in ubiquitin, but are, conserved between NEDD8 orthologs, are candidates for mediating, interactions with NEDD8-specific partners. One such residue, Ala-72 (Arg, in ubiquitin), is shown to perform a key role in selecting against, reaction with the ubiquitin E1 enzyme, thereby acting to prevent the, inappropriate diversion of NEDD8 into ubiquitin-specific pathways.
About this StructureAbout this Structure
1NDD is a Single protein structure of sequence from Homo sapiens with CL and SO4 as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the human ubiquitin-like protein NEDD8 and interactions with ubiquitin pathway enzymes., Whitby FG, Xia G, Pickart CM, Hill CP, J Biol Chem. 1998 Dec 25;273(52):34983-91. PMID:9857030
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