1B89
CLATHRIN HEAVY CHAIN PROXIMAL LEG SEGMENT (BOVINE)
Summary for 1B89
| Entry DOI | 10.2210/pdb1b89/pdb |
| Descriptor | PROTEIN (CLATHRIN HEAVY CHAIN) (1 entity in total) |
| Functional Keywords | clathrin, triskelion, coated vesicles, endocytosis, self-assembly, alpha-alpha superhelix |
| Biological source | Bos taurus (cattle) |
| Total number of polymer chains | 1 |
| Total formula weight | 52683.63 |
| Authors | Ybe, J.A.,Brodsky, F.M.,Hofmann, K.,Lin, K.,Liu, S.-H.,Chen, L.,Earnest, T.N.,Fletterick, R.J.,Hwang, P.K. (deposition date: 1999-05-27, release date: 1999-06-04, Last modification date: 2024-10-30) |
| Primary citation | Ybe, J.A.,Brodsky, F.M.,Hofmann, K.,Lin, K.,Liu, S.H.,Chen, L.,Earnest, T.N.,Fletterick, R.J.,Hwang, P.K. Clathrin self-assembly is mediated by a tandemly repeated superhelix. Nature, 399:371-375, 1999 Cited by PubMed Abstract: Clathrin is a triskelion-shaped cytoplasmic protein that polymerizes into a polyhedral lattice on intracellular membranes to form protein-coated membrane vesicles. Lattice formation induces the sorting of membrane proteins during endocytosis and organelle biogenesis by interacting with membrane-associated adaptor molecules. The clathrin triskelion is a trimer of heavy-chain subunits (1,675 residues), each binding a single light-chain subunit, in the hub domain (residues 1,074-1,675). Light chains negatively modulate polymerization so that intracellular clathrin assembly is adaptor-dependent. Here we report the atomic structure, to 2.6 A resolution, of hub residues 1,210-1,516 involved in mediating spontaneous clathrin heavy-chain polymerization and light-chain association. The hub fragment folds into an elongated coil of alpha-helices, and alignment analyses reveal a 145-residue motif that is repeated seven times along the filamentous leg and appears in other proteins involved in vacuolar protein sorting. The resulting model provides a three-dimensional framework for understanding clathrin heavy-chain self-assembly, light-chain binding and trimerization. PubMed: 10360576DOI: 10.1038/20708 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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