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TitleMolecular model for a complete clathrin lattice from electron cryomicroscopy.
Journal, issue, pagesNature, Vol. 432, Issue 7017, Page 573-579, Year 2004
Publish dateDec 2, 2004
AuthorsAlexander Fotin / Yifan Cheng / Piotr Sliz / Nikolaus Grigorieff / Stephen C Harrison / Tomas Kirchhausen / Thomas Walz /
PubMed AbstractClathrin-coated vesicles are important vehicles of membrane traffic in cells. We report the structure of a clathrin lattice at subnanometre resolution, obtained from electron cryomicroscopy of coats ...Clathrin-coated vesicles are important vehicles of membrane traffic in cells. We report the structure of a clathrin lattice at subnanometre resolution, obtained from electron cryomicroscopy of coats assembled in vitro. We trace most of the 1,675-residue clathrin heavy chain by fitting known crystal structures of two segments, and homology models of the rest, into the electron microscopy density map. We also define the position of the central helical segment of the light chain. A helical tripod, the carboxy-terminal parts of three heavy chains, projects inward from the vertex of each three-legged clathrin triskelion, linking that vertex to 'ankles' of triskelions centred two vertices away. Analysis of coats with distinct diameters shows an invariant pattern of contacts in the neighbourhood of each vertex, with more variable interactions along the extended parts of the triskelion 'legs'. These invariant local interactions appear to stabilize the lattice, allowing assembly and uncoating to be controlled by events at a few specific sites.
External linksNature / PubMed:15502812
MethodsEM (single particle)
Resolution7.9 Å
Structure data

5119

1xi4

3iyv

EMDB-5119: Clathrin D6 coat
PDB-1xi4: Clathrin D6 Coat
PDB-3iyv: Clathrin D6 coat as full-length Triskelions
Method: EM (single particle) / Resolution: 7.9 Å

Source
  • bos taurus (cattle)
KeywordsENDOCYTOSIS/EXOCYTOSIS / clathrin / alpha-zig-zag / beta-propeller / ENDOCYTOSIS-EXOCYTOSIS COMPLEX

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