5J45

Crystal structure of Shrub, fly ortholog of SNF7/CHMP4B

Summary for 5J45

• Entry DOI: 10.2210/pdb5j45/pdb
• Descriptor: GH13992p (1 entity in total)
• Functional Keywords: escrt, polymerization, membrane, transport protein
• Biological source: Drosophila melanogaster (Fruit fly)
• Total number of polymer chains: 1
• Total formula weight: 14754.85

Authors

McMillan, B.J.,Blacklow, S.C. (deposition date: 2016-03-31, release date: 2016-07-20, Last modification date: 2024-10-30)

Primary citation

McMillan, B.J.,Tibbe, C.,Jeon, H.,Drabek, A.A.,Klein, T.,Blacklow, S.C.
Electrostatic Interactions between Elongated Monomers Drive Filamentation of Drosophila Shrub, a Metazoan ESCRT-III Protein.
Cell Rep, 16:1211-1217, 2016

PubMed Abstract: The endosomal sorting complex required for transport (ESCRT) is a conserved protein complex that facilitates budding and fission of membranes. It executes a key step in many cellular events, including cytokinesis and multi-vesicular body formation. The ESCRT-III protein Shrub in flies, or its homologs in yeast (Snf7) or humans (CHMP4B), is a critical polymerizing component of ESCRT-III needed to effect membrane fission. We report the structural basis for polymerization of Shrub and define a minimal region required for filament formation. The X-ray structure of the Shrub core shows that individual monomers in the lattice interact in a staggered arrangement using complementary electrostatic surfaces. Mutations that disrupt interface salt bridges interfere with Shrub polymerization and function. Despite substantial sequence divergence and differences in packing interactions, the arrangement of Shrub subunits in the polymer resembles that of Snf7 and other family homologs, suggesting that this intermolecular packing mechanism is shared among ESCRT-III proteins.

PubMed: 27452459
DOI: 10.1016/j.celrep.2016.06.093

Experimental method

X-RAY DIFFRACTION (2.758 Å)