2EFL: Crystal Structure Of The Efc Domain Of Formin-binding Protein 17

Citation:
Abstract
Pombe Cdc15 homology (PCH) proteins play an important role in a variety of actin-based processes, including clathrin-mediated endocytosis (CME). The defining feature of the PCH proteins is an evolutionarily conserved EFC/F-BAR domain for membrane association and tubulation. In the present study, we solved the crystal structures of the EFC domains of human FBP17 and CIP4. The structures revealed a gently curved helical-bundle dimer of approximately 220 A in length, which forms filaments through end-to-end interactions in the crystals. The curved EFC dimer fits a tubular membrane with an approximately 600 A diameter. We subsequently proposed a model in which the curved EFC filament drives tubulation. In fact, striation of tubular membranes was observed by phase-contrast cryo-transmission electron microscopy, and mutations that impaired filament formation also impaired membrane tubulation and cell membrane invagination. Furthermore, FBP17 is recruited to clathrin-coated pits in the late stage of CME, indicating its physiological role.
PDB ID: 2EFLDownload
MMDB ID: 46112
PDB Deposition Date: 2007/2/23
Updated in MMDB: 2007/11
Experimental Method:
x-ray diffraction
Resolution: 2.61  Å
Source Organism:
Similar Structures:
Biological Unit for 2EFL: dimeric; determined by author and by software (PISA,PQS)
Molecular Components in 2EFL
Label Count Molecule
Proteins (2 molecules)
2
Formin-binding Protein 1(Gene symbol: FNBP1)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB
.