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6TZ9

CryoEM reconstruction of membrane-bound ESCRT-III filament composed of CHMP1B only

This is a non-PDB format compatible entry.
Summary for 6TZ9
Entry DOI10.2210/pdb6tz9/pdb
EMDB information20588 20589 20590 20591
DescriptorCharged multivesicular body protein 1b (1 entity in total)
Functional Keywordsmembrane remodeling, membrane-bound protein filament, escrt-iii, lipid binding protein
Biological sourceHomo sapiens (Human)
Total number of polymer chains26
Total formula weight575649.20
Authors
Nguyen, H.C.,Frost, A. (deposition date: 2019-08-11, release date: 2020-04-08, Last modification date: 2024-03-20)
Primary citationNguyen, H.C.,Talledge, N.,McCullough, J.,Sharma, A.,Moss 3rd, F.R.,Iwasa, J.H.,Vershinin, M.D.,Sundquist, W.I.,Frost, A.
Membrane constriction and thinning by sequential ESCRT-III polymerization.
Nat.Struct.Mol.Biol., 27:392-399, 2020
Cited by
PubMed Abstract: The endosomal sorting complexes required for transport (ESCRTs) mediate diverse membrane remodeling events. These typically require ESCRT-III proteins to stabilize negatively curved membranes; however, recent work has indicated that certain ESCRT-IIIs also participate in positive-curvature membrane-shaping reactions. ESCRT-IIIs polymerize into membrane-binding filaments, but the structural basis for negative versus positive membrane remodeling by these proteins remains poorly understood. To learn how certain ESCRT-IIIs shape positively curved membranes, we determined structures of human membrane-bound CHMP1B-only, membrane-bound CHMP1B + IST1, and IST1-only filaments by cryo-EM. Our structures show how CHMP1B first polymerizes into a single-stranded helical filament, shaping membranes into moderate-curvature tubules. Subsequently, IST1 assembles a second strand on CHMP1B, further constricting the membrane tube and reducing its diameter nearly to the fission point. Each step of constriction thins the underlying bilayer, lowering the barrier to membrane fission. Our structures reveal how a two-component, sequential polymerization mechanism drives membrane tubulation, constriction and bilayer thinning.
PubMed: 32251413
DOI: 10.1038/s41594-020-0404-x
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (6.2 Å)
Structure validation

226707

數據於2024-10-30公開中

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