Atomic structure of clathrin: a beta propeller terminal domain joins an alpha zigzag linker.
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.
ter Haar
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Department of Cell Biology and Center for Blood Research, Harvard Medical School, Boston, Massachusetts 02115-5701, USA.
Musacchio
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A
Harrison
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SC
Kirchhausen
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T
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
D019390:Arrestins; D002966:Clathrin; D010446:Peptide Fragments; D000071557:beta-Arrestins