2GD5

Structural basis for budding by the ESCRTIII factor CHMP3

Summary for 2GD5

• Entry DOI: 10.2210/pdb2gd5/pdb
• Descriptor: Charged multivesicular body protein 3 (1 entity in total)
• Functional Keywords: chmp3, escrt-iii, protein transport
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm, cytosol: Q9Y3E7
• Total number of polymer chains: 4
• Total formula weight: 84006.48

Authors

Muziol, T.M.,Pineda-Molina, E.,Ravelli, R.B.,Zamborlini, A.,Usami, Y.,Gottlinger, H.,Weissenhorn, W. (deposition date: 2006-03-15, release date: 2006-06-13, Last modification date: 2024-10-30)

Primary citation

Pineda-Molina, E.,Ravelli, R.B.,Zamborlini, A.,Usami, Y.,Weissenhorn, W.
Structural Basis for Budding by the ESCRT-III Factor CHMP3.
Dev.Cell, 10:821-830, 2006

PubMed Abstract: The vacuolar protein sorting machinery regulates multivesicular body biogenesis and is selectively recruited by enveloped viruses to support budding. Here we report the crystal structure of the human ESCRT-III protein CHMP3 at 2.8 A resolution. The core structure of CHMP3 folds into a flat helical arrangement that assembles into a lattice, mainly via two different dimerization modes, and unilaterally exposes a highly basic surface. The C terminus, the target for Vps4-induced ESCRT disassembly, extends from the opposite side of the membrane targeting region. Mutations within the basic and dimerization regions hinder bilayer interaction in vivo and reverse the dominant-negative effect of a truncated CHMP3 fusion protein on HIV-1 budding. Thus, the final steps in the budding process may include CHMP protein polymerization and lattice formation on membranes by employing different bilayer-recognizing surfaces, a function shared by all CHMP family members.

PubMed: 16740483
DOI: 10.1016/j.devcel.2006.03.013

Experimental method

X-RAY DIFFRACTION (2.8 Å)