4qt4

Crystal structure of Peptidyl-tRNA hydrolase from a Gram-positive bacterium, Streptococcus pyogenes at 2.19 Angstrom resolution shows the Closed Structure of the Substrate Binding Cleft

spinqualitylabelsall models 4qt4, resolution 2.19Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4qt4 is a 2 chain structure with sequence from Strpz. This structure supersedes the now removed PDB entry 4q55. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 4jc4 Gene: pth, Spy49_0005 (STRPZ) Activity: Aminoacyl-tRNA hydrolase, with EC number 3.1.1.29 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PTH_STRPZ] The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis (By similarity). Publication Abstract from PubMed Peptidyl-tRNA hydrolase (Pth) catalyses the release of tRNA and peptide components from peptidyl-tRNA molecules. Pth from a Gram-positive bacterium Streptococcus pyogenes (SpPth) was cloned, expressed, purified and crystallised. Three-dimensional structure of SpPth was determined by X-ray crystallography at 2.19 A resolution. Structure determination showed that the asymmetric unit of the unit cell contained two crystallographically independent molecules, designated A and B. The superimposition of C(alpha) traces of molecules A and B showed an r.m.s. shift of 0.4 A, indicating that the structures of two crystallographically independent molecules were identical. The polypeptide chain of SpPth adopted an overall alpha/beta conformation. The substrate-binding cleft in SpPth is formed with three loops: the gate loop, Ile91-Leu102; the base loop, Gly108-Gly115; and the lid loop, Gly136-Gly150. Unlike in the structures of Pth from Gram-negative bacteria, the entry to the cleft in the structure of SpPth appeared to be virtually closed. However, the conformations of the active site residues were found to be similar. Crystal structure of peptidyl-tRNA hydrolase from a Gram-positive bacterium, Streptococcus pyogenes at 2.19 A resolution shows the closed structure of the substrate-binding cleft.,Singh A, Gautam L, Sinha M, Bhushan A, Kaur P, Sharma S, Singh TP FEBS Open Bio. 2014 Oct 22;4:915-22. doi: 10.1016/j.fob.2014.10.010. eCollection , 2014. PMID:25389518 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Peptidyl-tRNA hydrolase

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