3F1I
Human ESCRT-0 Core Complex
Summary for 3F1I
Entry DOI | 10.2210/pdb3f1i/pdb |
Descriptor | Hepatocyte growth factor-regulated tyrosine kinase substrate, Signal transducing adapter molecule 1 (3 entities in total) |
Functional Keywords | hgs, stam, escrt, ubiquitin, mvb, endosome, membrane, metal-binding, phosphoprotein, protein transport, transport, zinc-finger, sh3 domain, protein binding |
Biological source | Homo sapiens (human) More |
Cellular location | Cytoplasm: O14964 Cytoplasm (Probable): Q92783 |
Total number of polymer chains | 3 |
Total formula weight | 29324.25 |
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 citation | Ren, 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: 19278655DOI: 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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