1X04

Crystal structure of endophilin BAR domain (mutant)

Summary for 1X04

• Entry DOI: 10.2210/pdb1x04/pdb
• Related: 1X03
• Descriptor: SH3-containing GRB2-like protein 2 (1 entity in total)
• Functional Keywords: bar domain, transferase
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm : Q99962
• Total number of polymer chains: 1
• Total formula weight: 26610.15

Authors

Masuda, M.,Takeda, S.,Sone, M.,Kamioka, Y.,Mori, H.,Mochizuki, N. (deposition date: 2005-03-14, release date: 2006-05-02, Last modification date: 2024-10-23)

Primary citation

Masuda, M.,Takeda, S.,Sone, M.,Ohki, T.,Mori, H.,Kamioka, Y.,Mochizuki, N.
Endophilin BAR domain drives membrane curvature by two newly identified structure-based mechanisms
Embo J., 25:2889-2897, 2006

PubMed Abstract: The crescent-shaped BAR (Bin/Amphiphysin/Rvs-homology) domain dimer is a versatile protein module that senses and generates positive membrane curvature. The BAR domain dimer of human endophilin-A1, solved at 3.1 A, has a unique structure consisting of a pair of helix-loop appendages sprouting out from the crescent. The appendage's short helices form a hydrophobic ridge, which runs across the concave surface at its center. Examining liposome binding and tubulation in vitro using purified BAR domain and its mutants indicated that the ridge penetrates into the membrane bilayer and enhances liposome tubulation. BAR domain-expressing cells exhibited marked plasma membrane tubulation in vivo. Furthermore, a swinging-arm mutant lost liposome tubulation activity yet retaining liposome binding. These data suggested that the rigid crescent dimer shape is crucial for the tubulation. We here propose that the BAR domain drives membrane curvature by coordinate action of the crescent's scaffold mechanism and the ridge's membrane insertion in addition to membrane binding via amino-terminal amphipathic helix.

PubMed: 16763557
DOI: 10.1038/sj.emboj.7601176

Experimental method

X-RAY DIFFRACTION (2.9 Å)