1s1q

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spinqualitylabelsall models 1s1q, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

TSG101(UEV) domain in complex with Ubiquitin

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

The UEV domain of the TSG101 protein functions in both HIV-1 budding and, the vacuolar protein sorting (VPS) pathway, where it binds ubiquitylated, proteins as they are sorted into vesicles that bud into late endosomal, compartments called multivesicular bodies (MVBs). TSG101 UEV-ubiquitin, interactions are therefore important for delivery of both substrates and, hydrolytic enzymes to lysosomes, which receive proteins via fusion with, MVBs. Here, we report the crystal structure of the TSG101 UEV domain in, complex with ubiquitin at 2.0 A resolution. TSG101 UEV contacts the Ile44, surface and an adjacent loop of ubiquitin through a highly solvated, interface. Mutations that disrupt the interface inhibit MVB sorting, and, the structure also explains how the TSG101 UEV can independently bind its, ubiquitin and Pro-Thr/Ser-Ala-Pro peptide ligands. Remarkably, comparison, with mapping data from other UEV and related E2 proteins indicates that, although the different E2/UEV domains share the same structure and have, conserved ubiquitin binding activity, they bind through very different, interfaces.

Disease

Known disease associated with this structure: Breast cancer OMIM:[601387]

About this Structure

1S1Q is a Protein complex structure of sequences from Homo sapiens with CU, SO4 and ACY as ligands. Full crystallographic information is available from OCA.

Reference

Ubiquitin recognition by the human TSG101 protein., Sundquist WI, Schubert HL, Kelly BN, Hill GC, Holton JM, Hill CP, Mol Cell. 2004 Mar 26;13(6):783-9. PMID:15053872

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