2CAY

Vps36 N-terminal PH domain

Summary for 2CAY

• Entry DOI: 10.2210/pdb2cay/pdb
• Related: 1U5T 1W7P
• Descriptor: VACUOLAR PROTEIN SORTING PROTEIN 36, SULFATE ION (3 entities in total)
• Functional Keywords: transport, vps36, ph domain, escrt-ii, lipid-binding, multivesicular bodies, membrane, metal-binding, protein transport, zinc, zinc-finger
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• Cellular location: Cytoplasm : Q06696
• Total number of polymer chains: 2
• Total formula weight: 33978.16

Authors

Teo, H.,Williams, R.L.,Perisic, O.,Gill, D.J. (deposition date: 2005-12-23, release date: 2006-04-07, Last modification date: 2024-05-08)

Primary citation

Teo, H.,Gill, D.J.,Sun, J.,Perisic, O.,Veprintsev, D.B.,Wallis, Y.,Emr, S.D.,Williams, R.L.
Escrt-I Core and Escrt-II Glue Domain Structures Reveal Role for Glue in Linking to Escrt-I and Membranes.
Cell(Cambridge,Mass.), 125:99-, 2006

PubMed Abstract: ESCRT complexes form the main machinery driving protein sorting from endosomes to lysosomes. Currently, the picture regarding assembly of ESCRTs on endosomes is incomplete. The structure of the conserved heterotrimeric ESCRT-I core presented here shows a fan-like arrangement of three helical hairpins, each corresponding to a different subunit. Vps23/Tsg101 is the central hairpin sandwiched between the other subunits, explaining the critical role of its "steadiness box" in the stability of ESCRT-I. We show that yeast ESCRT-I links directly to ESCRT-II, through a tight interaction of Vps28 (ESCRT-I) with the yeast-specific zinc-finger insertion within the GLUE domain of Vps36 (ESCRT-II). The crystal structure of the GLUE domain missing this insertion reveals it is a split PH domain, with a noncanonical lipid binding pocket that binds PtdIns3P. The simultaneous and reinforcing interactions of ESCRT-II GLUE domain with membranes, ESCRT-I, and ubiquitin are critical for ubiquitinated cargo progression from early to late endosomes.

PubMed: 16615893
DOI: 10.1016/J.CELL.2006.01.047

Experimental method

X-RAY DIFFRACTION (1.9 Å)