| Literature DB >> 19278655 |
Xuefeng Ren1, Daniel P Kloer, Young C Kim, Rodolfo Ghirlando, Layla F Saidi, Gerhard Hummer, James H Hurley.
Abstract
The human Hrs and STAM proteins comprise the ESCRT-0 complex, which sorts ubiquitinated cell surface receptors to lysosomes for degradation. Here we report a model for the complete ESCRT-0 complex based on the crystal structure of the Hrs-STAM core complex, previously solved domain structures, hydrodynamic measurements, and Monte Carlo simulations. ESCRT-0 expressed in insect cells has a hydrodynamic radius of RH = 7.9 nm and is a 1:1 heterodimer. The 2.3 Angstroms crystal structure of the ESCRT-0 core complex reveals two domain-swapped GAT domains and an antiparallel two-stranded coiled-coil, similar to yeast ESCRT-0. ESCRT-0 typifies a class of biomolecular assemblies that combine structured and unstructured elements, and have dynamic and open conformations to ensure versatility in target recognition. Coarse-grained Monte Carlo simulations constrained by experimental RH values for ESCRT-0 reveal a dynamic ensemble of conformations well suited for diverse functions.Entities:
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Year: 2009 PMID： 19278655 PMCID： PMC2676576 DOI： 10.1016/j.str.2009.01.012
Source DB: PubMed Journal: Structure ISSN： 0969-2126 Impact factor: 5.006