2g3q
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Solution Structure of Ede1 UBA-ubiquitin complex
OverviewOverview
Monoubiquitination is a general mechanism for downregulating the activity, of cell surface receptors by consigning these proteins for, lysosome-mediated degradation through the endocytic pathway. The yeast, Ede1 protein functions at the internalization step of endocytosis and, binds monoubiquitinated proteins through a ubiquitin associated (UBA), domain. UBA domains are found in a broad range of cellular proteins but, previous studies have suggested that the mode of ubiquitin recognition, might not be universally conserved. Here we present the solution structure, of the Ede1 UBA domain in complex with monoubiquitin. The Ede1 UBA domain, forms a three-helix bundle structure and binds ubiquitin through a largely, hydrophobic surface in a manner reminiscent of the Dsk2 UBA and the, remotely homologous Cue2 CUE domains, for which high-resolution structures, have been described. However, the interaction is dissimilar to the, molecular models proposed for the hHR23A UBA domains bound to either, monoubiquitin or Lys48-linked diubiquitin. Our mutational analyses of the, Ede1 UBA domain-ubiquitin interaction reveal several key affinity, determinants and, unexpectedly, a negative affinity determinant in the, wild-type Ede1 protein, implying that high-affinity interactions may not, be the sole criterion for optimal function of monoubiquitin-binding, endocytic proteins.
About this StructureAbout this Structure
2G3Q is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for monoubiquitin recognition by the Ede1 UBA domain., Swanson KA, Hicke L, Radhakrishnan I, J Mol Biol. 2006 May 5;358(3):713-24. Epub 2006 Mar 9. PMID:16563434
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