2efk
From Proteopedia
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| - | [[Image:2efk.jpg|left|200px]] | + | [[Image:2efk.jpg|left|200px]] |
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| - | '''Crystal structure of the EFC domain of Cdc42-interacting protein 4''' | + | {{Structure |
| + | |PDB= 2efk |SIZE=350|CAPTION= <scene name='initialview01'>2efk</scene>, resolution 2.30Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Crystal structure of the EFC domain of Cdc42-interacting protein 4''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2EFK is a [ | + | 2EFK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EFK OCA]. |
==Reference== | ==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:[http:// | + | 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://www.ncbi.nlm.nih.gov/pubmed/17512409 17512409] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Yokoyama, S.]] | [[Category: Yokoyama, S.]] | ||
[[Category: efc domain]] | [[Category: efc domain]] | ||
| - | [[Category: national project on protein structural and functional | + | [[Category: national project on protein structural and functional analyse]] |
[[Category: nppsfa]] | [[Category: nppsfa]] | ||
[[Category: riken structural genomics/proteomics initiative]] | [[Category: riken structural genomics/proteomics initiative]] | ||
[[Category: rsgi]] | [[Category: rsgi]] | ||
| - | [[Category: structural | + | [[Category: structural genomic]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:39:26 2008'' |
Revision as of 14:39, 20 March 2008
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| , resolution 2.30Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Mar 20 16:39:26 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 analyse | Nppsfa | Riken structural genomics/proteomics initiative | Rsgi | Structural genomic
