3LDZ

Crystal structure of human STAM1 VHS domain in complex with ubiquitin

Summary for 3LDZ

• Entry DOI: 10.2210/pdb3ldz/pdb
• Descriptor: Ubiquitin, Signal transducing adapter molecule 1 (2 entities in total)
• Functional Keywords: ubiquitin-binding, cytoplasm, ubl conjugation, endosome, membrane, protein transport, sh3 domain, transport
• Biological source: Bos taurus (bovine); More
• Cellular location: Cytoplasm : Q92783
• Total number of polymer chains: 7
• Total formula weight: 87544.66

Authors

Ren, X.,Hurley, J.H. (deposition date: 2010-01-13, release date: 2010-03-02, Last modification date: 2024-02-21)

Primary citation

Ren, X.,Hurley, J.H.
VHS domains of ESCRT-0 cooperate in high-avidity binding to polyubiquitinated cargo.
Embo J., 29:1045-1054, 2010

PubMed Abstract: VHS (Vps27, Hrs, and STAM) domains occur in ESCRT-0 subunits Hrs and STAM, GGA adapters, and other trafficking proteins. The structure of the STAM VHS domain-ubiquitin complex was solved at 2.6 A resolution, revealing that determinants for ubiquitin recognition are conserved in nearly all VHS domains. VHS domains from all classes of VHS-domain containing proteins in yeast and humans, including both subunits of ESCRT-0, bound ubiquitin in vitro. ESCRTs have been implicated in the sorting of Lys63-linked polyubiquitinated cargo. Intact human ESCRT-0 binds Lys63-linked tetraubiquitin 50-fold more tightly than monoubiquitin, though only 2-fold more tightly than Lys48-linked tetraubiquitin. The gain in affinity is attributed to the cooperation of flexibly connected VHS and UIM motifs of ESCRT-0 in avid binding to the polyubiquitin chain. Mutational analysis of all the five ubiquitin-binding sites in yeast ESCRT-0 shows that cooperation between them is required for the sorting of the Lys63-linked polyubiquitinated cargo Cps1 to the vacuole.

PubMed: 20150893
DOI: 10.1038/emboj.2010.6

Experimental method

X-RAY DIFFRACTION (2.6 Å)