Abstract
The endosomal sorting complex required for transport (ESCRT) complexes are central to receptor downregulation, lysosome biogenesis, and budding of HIV. The yeast ESCRT-I complex contains the Vps23, Vps28, and Vps37 proteins, and its assembly is directed by the C-terminal steadiness box of Vps23, the N-terminal half of Vps28, and the C-terminal half of Vps37. The crystal structures of a Vps23:Vps28 core subcomplex and the Vps23:Vps28:Vps37 core were solved at 2.1 and 2.8 A resolution. Each subunit contains a structurally similar pair of helices that form the core. The N-terminal domain of Vps28 has a hydrophobic binding site on its surface that is conformationally dynamic. The C-terminal domain of Vps28 binds the ESCRT-II complex. The structure shows how ESCRT-I is assembled by a compact core from which the Vps23 UEV domain, the Vps28 C domain, and other domains project to bind their partners.
Publication types
-
Research Support, N.I.H., Extramural
-
Research Support, Non-U.S. Gov't
-
Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
-
Amino Acid Motifs
-
Amino Acid Sequence
-
Endosomal Sorting Complexes Required for Transport
-
Models, Molecular
-
Molecular Sequence Data
-
Phenotype
-
Protein Conformation
-
Protein Interaction Mapping
-
Protein Transport
-
Recombinant Fusion Proteins / metabolism
-
Saccharomyces cerevisiae / cytology
-
Saccharomyces cerevisiae / metabolism*
-
Saccharomyces cerevisiae Proteins / chemistry*
-
Saccharomyces cerevisiae Proteins / metabolism*
-
Sequence Alignment
-
Vesicular Transport Proteins / chemistry*
-
Vesicular Transport Proteins / metabolism*
Substances
-
Endosomal Sorting Complexes Required for Transport
-
Recombinant Fusion Proteins
-
SRN2 protein, S cerevisiae
-
STP22 protein, S cerevisiae
-
Saccharomyces cerevisiae Proteins
-
VPS28 protein, S cerevisiae
-
Vesicular Transport Proteins