3LVH
Crystal structure of a clathrin heavy chain and clathrin light chain complex
Summary for 3LVH
| Entry DOI | 10.2210/pdb3lvh/pdb |
| Related | 3LVG |
| Descriptor | Clathrin heavy chain 1, Clathrin light chain B (2 entities in total) |
| Functional Keywords | self assembly, coated pit, cytoplasmic vesicle, membrane, calcium, structural protein |
| Biological source | Bos taurus (bovine,cow,domestic cattle,domestic cow) More |
| Cellular location | Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side: P49951 |
| Total number of polymer chains | 6 |
| Total formula weight | 281053.57 |
| Authors | Wilbur, J.D.,Hwang, P.K.,Ybe, J.A.,Lane, M.,Sellers, B.D.,Jacobson, M.P.,Fletterick, R.J.,Brodsky, F.M. (deposition date: 2010-02-20, release date: 2010-06-09, Last modification date: 2024-02-21) |
| Primary citation | Wilbur, J.D.,Hwang, P.K.,Ybe, J.A.,Lane, M.,Sellers, B.D.,Jacobson, M.P.,Fletterick, R.J.,Brodsky, F.M. Conformation switching of clathrin light chain regulates clathrin lattice assembly. Dev.Cell, 18:841-848, 2010 Cited by PubMed Abstract: Clathrin-coated vesicle formation is responsible for membrane traffic to and from the endocytic pathway during receptor-mediated endocytosis and organelle biogenesis, influencing how cells relate to their environment. Generating these vesicles involves self-assembly of clathrin molecules into a latticed coat on membranes that recruits receptors and organizes protein machinery necessary for budding. Here we define a molecular mechanism regulating clathrin lattice formation by obtaining structural information from co-crystals of clathrin subunits. Low resolution X-ray diffraction data (7.9-9.0 A) was analyzed using a combination of molecular replacement with an energy-minimized model and noncrystallographic symmetry averaging. Resulting topological information revealed two conformations of the regulatory clathrin light chain bound to clathrin heavy chain. Based on protein domain positions, mutagenesis, and biochemical assays, we identify an electrostatic interaction between the clathrin subunits that allows the observed conformational variation in clathrin light chains to alter the conformation of the clathrin heavy chain and thereby regulates assembly. PubMed: 20493816DOI: 10.1016/j.devcel.2010.04.007 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (9 Å) |
Structure validation
Download full validation report
