2efl: Difference between revisions
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|PDB= 2efl |SIZE=350|CAPTION= <scene name='initialview01'>2efl</scene>, resolution 2.61Å | |PDB= 2efl |SIZE=350|CAPTION= <scene name='initialview01'>2efl</scene>, resolution 2.61Å | ||
|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2efl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2efl OCA], [http://www.ebi.ac.uk/pdbsum/2efl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2efl RCSB]</span> | |||
}} | }} | ||
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[[Category: structural genomic]] | [[Category: structural genomic]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:48:17 2008'' | ||
Revision as of 02:48, 31 March 2008
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| , resolution 2.61Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the EFC domain of formin-binding protein 17
OverviewOverview
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 StructureAbout this Structure
2EFL is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- Homo sapiens
- Single protein
- Niwa, H.
- RSGI, RIKEN Structural Genomics/Proteomics Initiative.
- Shimada, A.
- Shirouzu, M.
- Terada, T.
- Yokoyama, S.
- Efc domain
- National project on protein structural and functional analyse
- Nppsfa
- Riken structural genomics/proteomics initiative
- Rsgi
- Structural genomic