2P22: Structure of the Yeast ESCRT-I Heterotetramer Core

Citation:
Abstract
The endosomal sorting complex required for transport-I (ESCRT-I) complex, which is conserved from yeast to humans, directs the lysosomal degradation of ubiquitinated transmembrane proteins and the budding of the HIV virus. Yeast ESCRT-I contains four subunits, Vps23, Vps28, Vps37, and Mvb12. The crystal structure of the heterotetrameric ESCRT-I complex reveals a highly asymmetric complex of 1:1:1:1 subunit stoichiometry. The core complex is nearly 18 nm long and consists of a headpiece attached to a 13 nm stalk. The stalk is important for cargo sorting by ESCRT-I and is proposed to serve as a spacer regulating the correct disposition of cargo and other ESCRT components. Hydrodynamic constraints and crystallographic structures were used to generate a model of intact ESCRT-I in solution. The results show how ESCRT-I uses a combination of a rigid stalk and flexible tethers to interact with lipids, cargo, and other ESCRT complexes over a span of approximately 25 nm.
PDB ID: 2P22Download
MMDB ID: 46484
PDB Deposition Date: 2007/3/6
Updated in MMDB: 2017/12
Experimental Method:
x-ray diffraction
Resolution: 2.7  Å
Source Organism:
Similar Structures:
Biological Unit for 2P22: tetrameric; determined by author and by software (PISA)
Molecular Components in 2P22
Label Count Molecule
Proteins (4 molecules)
1
Suppressor Protein Stp22 of Temperature-sensitive Alpha-factor Receptor and Arginine Permease(Gene symbol: STP22)
Molecule annotation
1
Vacuolar Protein Sorting-associated Protein 28(Gene symbol: VPS28)
Molecule annotation
1
Protein Srn2(Gene symbol: SRN2)
Molecule annotation
1
Hypothetical 12.0 KDA Protein in Ade3-ser2 Intergenic Region(Gene symbol: MVB12)
Molecule annotation
Chemicals (4 molecules)
1
4
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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