title: Atomic structure of clathrin: a beta propeller terminal domain joins an alpha zigzag linker.
abstract: Clathrin triskelions form the lattice that organizes recruitment of proteins to coated pits and helps drive vesiculation of the lipid bilayer. We report the crystal structure at 2.6 A resolution of a 55 kDa N-terminal fragment from the 190 kDa clathrin heavy chain. The structure comprises the globular "terminal domain" and the linker that joins it to the end of a triskelion leg. The terminal domain is a seven-blade beta propeller, a structure well adapted to interaction with multiple partners, such as the AP-1 and AP-2 sorting adaptor complexes and the nonvisual arrestins. The linker is an alpha-helical zigzag emanating from the propeller domain. We propose that this simple motif may extend into the rest of the clathrin leg.
authors.affiliation: Department of Cell Biology and Center for Blood Research, Harvard Medical School, Boston, Massachusetts 02115-5701, USA.
authors.forename: E
authors.initials: E
authors.lastname: ter Haar
authors.forename: A
authors.initials: A
authors.lastname: Musacchio
authors.forename: S C
authors.initials: SC
authors.lastname: Harrison
authors.forename: T
authors.initials: T
authors.lastname: Kirchhausen
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D019390:Arrestins / Q000378:metabolism; D002966:Clathrin / Q000737:chemistry* / Q000378:metabolism; D018360:Crystallography, X-Ray; D018257:Helix-Loop-Helix Motifs; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry* / Q000378:metabolism; D017434:Protein Structure, Tertiary; D051381:Rats; D000071557:beta-Arrestins
chemical_list: D019390:Arrestins; D002966:Clathrin; D010446:Peptide Fragments; D000071557:beta-Arrestins