3LXU
Crystal Structure of Tripeptidyl Peptidase 2 (TPP II)
Summary for 3LXU
| Entry DOI | 10.2210/pdb3lxu/pdb |
| Descriptor | Tripeptidyl-peptidase 2 (1 entity in total) |
| Functional Keywords | spindle complex, aminopeptidase, hydrolase, phosphoprotein, serine protease |
| Biological source | Drosophila melanogaster (Fruit fly) |
| Cellular location | Cytoplasm (Probable): Q9V6K1 |
| Total number of polymer chains | 1 |
| Total formula weight | 150406.61 |
| Authors | Chuang, C.K. (deposition date: 2010-02-25, release date: 2010-08-11, Last modification date: 2024-10-16) |
| Primary citation | Chuang, C.K.,Rockel, B.,Seyit, G.,Walian, P.J.,Schonegge, A.M.,Peters, J.,Zwart, P.H.,Baumeister, W.,Jap, B.K. Hybrid molecular structure of the giant protease tripeptidyl peptidase II. Nat.Struct.Mol.Biol., 17:990-996, 2010 Cited by PubMed Abstract: Tripeptidyl peptidase II (TPP II) is the largest known eukaryotic protease (6 MDa). It is believed to act downstream of the 26S proteasome, cleaving tripeptides from the N termini of longer peptides, and it is implicated in numerous cellular processes. Here we report the structure of Drosophila TPP II determined by a hybrid approach. We solved the structure of the dimer by X-ray crystallography and docked it into the three-dimensional map of the holocomplex, which we obtained by single-particle cryo-electron microscopy. The resulting structure reveals the compartmentalization of the active sites inside a system of chambers and suggests the existence of a molecular ruler determining the size of the cleavage products. Furthermore, the structure suggests a model for activation of TPP II involving the relocation of a flexible loop and a repositioning of the active-site serine, coupling it to holocomplex assembly and active-site sequestration. PubMed: 20676100DOI: 10.1038/nsmb.1870 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.14 Å) |
Structure validation
Download full validation report
