3lxu | pdb_00003lxu

Crystal Structure of Tripeptidyl Peptidase 2 (TPP II)

spinqualitylabelsall models 3lxu, resolution 3.14Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3lxu is a 1 chain structure with sequence from Drosophila melanogaster. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.14Å Ligands: MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TPP2_DROME Component of the proteolytic cascade acting downstream of the 26S proteasome in the ubiquitin-proteasome pathway. May be able to complement the 26S proteasome function to some extent under conditions in which the latter is inhibited (By similarity). Efficiently cleaves Ala-Ala-Ala-polypeptide and Pro-Pro-Ala-polypeptide, Val-Leu-Lys-polypeptide only at high concentration. Does not cleave Ala-Phe-Pro-polypeptide nor Pro-Leu-Gly-polypeptide. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Hybrid molecular structure of the giant protease tripeptidyl peptidase II.,Chuang CK, Rockel B, Seyit G, Walian PJ, Schonegge AM, Peters J, Zwart PH, Baumeister W, Jap BK Nat Struct Mol Biol. 2010 Aug;17(8):990-6. Epub 2010 Aug 1. PMID:20676100 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Tripeptidyl peptidase

Proteopedia Page Contributors and Editors (what is this?)

OCA