1tsp | pdb_00001tsp

CRYSTAL STRUCTURE OF P22 TAILSPIKE PROTEIN: INTERDIGITATED SUBUNITS IN A THERMOSTABLE TRIMER

spinqualitylabelsall models 1tsp, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1tsp is a 1 chain structure with sequence from Enterobacteria phage p22. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [TSPE_BPP22] Non-covalently bound to the neck of the phage capsid and mediating attachment of the viral particle to host cell-surface polysaccharide. It displays endorhamnosidase enzymatic activity, hydrolyzing the alpha-1,3-O-glycosidic linkage between rhamnose and galactose of the O-antigen polysaccharide. Publication Abstract from PubMed The tailspike protein (TSP) of Salmonella typhimurium phage P22 is a part of the apparatus by which the phage attaches to the bacterial host and hydrolyzes the O antigen. It has served as a model system for genetic and biochemical analysis of protein folding. The x-ray structure of a shortened TSP (residues 109 to 666) was determined to a 2.0 angstrom resolution. Each subunit of the homotrimer contains a large parallel beta helix. The interdigitation of the polypeptide chains at the carboxyl termini is important to protrimer formation in the folding pathway and to thermostability of the mature protein. Crystal structure of P22 tailspike protein: interdigitated subunits in a thermostable trimer.,Steinbacher S, Seckler R, Miller S, Steipe B, Huber R, Reinemer P Science. 1994 Jul 15;265(5170):383-6. PMID:8023158 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Tailspike protein

Proteopedia Page Contributors and Editors (what is this?)

OCA