2efk
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Pombe Cdc15 homology (PCH) proteins play an important role in a variety of | + | 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== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | Curved EFC/F-BAR- | + | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17512409 17512409] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Chen, L.]] | [[Category: Chen, L.]] | ||
| - | [[Category: Liu, Z | + | [[Category: Liu, Z J.]] |
[[Category: Niwa, H.]] | [[Category: Niwa, H.]] | ||
| - | [[Category: RSGI, RIKEN | + | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] |
[[Category: Shimada, A.]] | [[Category: Shimada, A.]] | ||
[[Category: Shirouzu, M.]] | [[Category: Shirouzu, M.]] | ||
[[Category: Terada, T.]] | [[Category: Terada, T.]] | ||
| - | [[Category: Wang, B | + | [[Category: Wang, B C.]] |
[[Category: Yokoyama, S.]] | [[Category: Yokoyama, S.]] | ||
[[Category: efc domain]] | [[Category: efc domain]] | ||
| Line 29: | Line 29: | ||
[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:09:36 2008'' |
Revision as of 15:09, 21 February 2008
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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
Page seeded by OCA on Thu Feb 21 17:09:36 2008
Categories: Homo sapiens | Single protein | Chen, L. | Liu, Z J. | Niwa, H. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Shimada, A. | Shirouzu, M. | Terada, T. | Wang, B C. | Yokoyama, S. | Efc domain | National project on protein structural and functional analyses | Nppsfa | Riken structural genomics/proteomics initiative | Rsgi | Structural genomics
