1q0v
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Solution Structure of Tandem UIMs of Vps27
OverviewOverview
Monoubiquitylation is a well-characterized signal for the internalization, and sorting of integral membrane proteins to distinct cellular organelles., Recognition and transmission of monoubiquitin signals is mediated by a, variety of ubiquitin-binding motifs such as UIM, UBA, UEV, VHS and CUE in, endocytic proteins. The yeast Vps27 protein requires two UIMs for, efficient interactions with ubiquitin and for sorting cargo into, multivesicular bodies. Here we show that the individual UIMs of Vps27, exist as autonomously folded alpha-helices that bind ubiquitin, independently, non-cooperatively and with modest affinity. The Vps27, N-terminal UIM engages the Leu8-Ile44-Val70 hydrophobic patch of ubiquitin, through a helical surface conserved in UIMs of diverse proteins, including, that of the S5a proteasomal regulatory subunit. The Leu8-Ile44-Val70, ubiquitin surface is also the site of interaction for CUE and UBA domains, in endocytic proteins, consistent with the view that ubiquitin-binding, endocytic proteins act serially on the same monoubiquitylated cargo during, transport from cell surface to the lysosome.
About this StructureAbout this Structure
1Q0V is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
Solution structure of Vps27 UIM-ubiquitin complex important for endosomal sorting and receptor downregulation., Swanson KA, Kang RS, Stamenova SD, Hicke L, Radhakrishnan I, EMBO J. 2003 Sep 15;22(18):4597-606. PMID:12970172
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