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3F1I

Human ESCRT-0 Core Complex

Summary for 3F1I
Entry DOI10.2210/pdb3f1i/pdb
DescriptorHepatocyte growth factor-regulated tyrosine kinase substrate, Signal transducing adapter molecule 1 (3 entities in total)
Functional Keywordshgs, stam, escrt, ubiquitin, mvb, endosome, membrane, metal-binding, phosphoprotein, protein transport, transport, zinc-finger, sh3 domain, protein binding
Biological sourceHomo sapiens (human)
More
Cellular locationCytoplasm: O14964
Cytoplasm (Probable): Q92783
Total number of polymer chains3
Total formula weight29324.25
Authors
Ren, X.,Kloer, D.P.,Kim, Y.,Ghirlando, R.,Saidi, L.,Hummer, G.,Hurley, J.H. (deposition date: 2008-10-28, release date: 2009-03-24, Last modification date: 2023-12-27)
Primary citationRen, X.,Kloer, D.P.,Kim, Y.C.,Ghirlando, R.,Saidi, L.F.,Hummer, G.,Hurley, J.H.
Hybrid Structural Model of the Complete Human ESCRT-0 Complex.
Structure, 17:406-416, 2009
Cited by
PubMed 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.
PubMed: 19278655
DOI: 10.1016/j.str.2009.01.012
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

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