1Q0V

Solution Structure of Tandem UIMs of Vps27

Summary for 1Q0V

• Entry DOI: 10.2210/pdb1q0v/pdb
• Related: 1O06
• Descriptor: hydrophilic protein; has cysteine rich putative zinc finger essential for function; Vps27p (1 entity in total)
• Functional Keywords: stable, non-interacting alpha-helices, transport binding
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Endosome membrane; Peripheral membrane protein; Cytoplasmic side: P40343
• Total number of polymer chains: 1
• Total formula weight: 9370.26

Authors

Swanson, K.A.,Kang, R.S.,Stamenova, S.D.,Hicke, L.,Radhakrishnan, I. (deposition date: 2003-07-17, release date: 2003-12-23, Last modification date: 2024-05-22)

Primary citation

Swanson, K.A.,Kang, R.S.,Stamenova, S.D.,Hicke, L.,Radhakrishnan, I.
Solution structure of Vps27 UIM-ubiquitin complex important for endosomal sorting and receptor downregulation.
Embo J., 22:4597-4606, 2003

PubMed Abstract: 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.

PubMed: 12970172
DOI: 10.1093/emboj/cdg471

Experimental method

SOLUTION NMR