4AE4

The UBAP1 subunit of ESCRT-I interacts with ubiquitin via a novel SOUBA domain

Summary for 4AE4

• Entry DOI: 10.2210/pdb4ae4/pdb
• Related: 1WGN
• Descriptor: UBIQUITIN-ASSOCIATED PROTEIN 1, 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID, POTASSIUM ION, ... (7 entities in total)
• Functional Keywords: protein transport, endosomal sorting, tetherin, vpu, hiv-1, monoubiquitin
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Cytoplasm, cytosol : Q9NZ09 Q9NZ09
• Total number of polymer chains: 2
• Total formula weight: 28318.82

Authors

Agromayor, M.,Soler, N.,Caballe, A.,Kueck, T.,Freund, S.M.,Allen, M.D.,Bycroft, M.,Perisic, O.,Ye, Y.,McDonald, B.,Scheel, H.,Hofmann, K.,Neil, S.J.D.,Martin-Serrano, J.,Williams, R.L. (deposition date: 2012-01-06, release date: 2012-03-21, Last modification date: 2025-04-09)

Primary citation

Agromayor, M.,Soler, N.,Caballe, A.,Kueck, T.,Freund, S.M.,Allen, M.D.,Bycroft, M.,Perisic, O.,Ye, Y.,McDonald, B.,Scheel, H.,Hofmann, K.,Neil, S.J.,Martin-Serrano, J.,Williams, R.L.
The UBAP1 subunit of ESCRT-I interacts with ubiquitin via a SOUBA domain.
Structure, 20:414-428, 2012

PubMed Abstract: The endosomal sorting complexes required for transport (ESCRTs) facilitate endosomal sorting of ubiquitinated cargo, MVB biogenesis, late stages of cytokinesis, and retroviral budding. Here we show that ubiquitin associated protein 1 (UBAP1), a subunit of human ESCRT-I, coassembles in a stable 1:1:1:1 complex with Vps23/TSG101, VPS28, and VPS37. The X-ray crystal structure of the C-terminal region of UBAP1 reveals a domain that we describe as a solenoid of overlapping UBAs (SOUBA). NMR analysis shows that each of the three rigidly arranged overlapping UBAs making up the SOUBA interact with ubiquitin. We demonstrate that UBAP1-containing ESCRT-I is essential for degradation of antiviral cell-surface proteins, such as tetherin (BST-2/CD317), by viral countermeasures, namely, the HIV-1 accessory protein Vpu and the Kaposi sarcoma-associated herpesvirus (KSHV) ubiquitin ligase K5.

PubMed: 22405001
DOI: 10.1016/j.str.2011.12.013

Experimental method

X-RAY DIFFRACTION (1.65 Å)