2efk

From Proteopedia

Revision as of 13:05, 23 January 2008

Crystal structure of the EFC domain of Cdc42-interacting protein 4

Overview

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.

About this Structure

2EFK is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Curved EFC/F-BAR-Domain Dimers Are Joined End to End into a Filament for Membrane Invagination in Endocytosis., Shimada A, Niwa H, Tsujita K, Suetsugu S, Nitta K, Hanawa-Suetsugu K, Akasaka R, Nishino Y, Toyama M, Chen L, Liu ZJ, Wang BC, Yamamoto M, Terada T, Miyazawa A, Tanaka A, Sugano S, Shirouzu M, Nagayama K, Takenawa T, Yokoyama S, Cell. 2007 May 18;129(4):761-72. PMID:17512409

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