1pys

PHENYLALANYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUSPHENYLALANYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS

Structural highlights 1pys is a 2 chain structure with sequence from Thermus thermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: Activity: Phenylalanine--tRNA ligase, with EC number 6.1.1.20 Resources: FirstGlance, OCA, RCSB, PDBsum 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 The crystal structure of phenylalanyl-tRNA synthetase from Thermus thermophilus, solved at 2.9 A resolution, displays (alpha beta)2 subunit organization. Unexpectedly, both the catalytic alpha- and the non-catalytic beta-subunits comprise the characteristic fold of the class II active-site domains. The alpha beta heterodimer contains most of the building blocks so far identified in the class II synthetases. The presence of an RNA-binding domain, similar to that of the U1A spliceosomal protein, in the beta-subunit is indicative of structural relationships among different families of RNA-binding proteins. The structure suggests a plausible catalytic mechanism which explains why the primary site of tRNA aminoacylation is different from that of the other class II enzymes. Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus.,Mosyak L, Reshetnikova L, Goldgur Y, Delarue M, Safro MG Nat Struct Biol. 1995 Jul;2(7):537-47. PMID:7664121 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aminoacyl tRNA Synthetase

spinqualitylabelsall models 1pys, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image