Functional organization of clathrin in coats: combining electron cryomicroscopy and X-ray crystallography.
The sorting of specific proteins into clathrin-coated pits and the mechanics of membrane invagination are determined by assembly of the clathrin lattice. Recent structures of a six-fold barrel clathrin coat at 21 A resolution by electron cryomicroscopy and of the clathrin terminal domain and linker at 2.6 A by X-ray crystallography together show how domains of clathrin interact and orient within the coat and reveal the strongly puckered shape and conformational variability of individual triskelions. The beta propeller of the terminal domain faces the membrane so that recognition segments from adaptor proteins can extend along its lateral grooves. Clathrin legs adapt to different coat environments in the barrel by flexing along a segment at the knee that is free of contacts with other molecules.
Children's Hospital, Harvard Medical School, Boston, Massachusetts 02115, USA.
A
A
Musacchio
C J
CJ
Smith
A M
AM
Roseman
S C
SC
Harrison
T
T
Kirchhausen
B M
BM
Pearse
D002966:Clathrin / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D033922:Clathrin Heavy Chains; D003034:Coated Pits, Cell-Membrane / Q000737:chemistry / Q000648:ultrastructure*; D018699:Coated Vesicles / Q000737:chemistry / Q000648:ultrastructure*; D020285:Cryoelectron Microscopy; D003460:Crystallization; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D018583:Pliability; D011485:Protein Binding; D011487:Protein Conformation
D002966:Clathrin; D033922:Clathrin Heavy Chains