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Publication Abstract from PubMed

Peptidyl-tRNA hydrolase (Pth) catalyzes the release of tRNA to relieve peptidyl-tRNA accumulation. Because Pth activity is essential for the viability of bacteria, Pth is regarded as a promising target for the discovery of new antimicrobial agents. Here, the structure of Pth from the Gram-positive bacterium Staphylococcus aureus (SaPth) was solved by X-ray crystallography at a 2.25 A resolution. The SaPth structure exhibits significant structural similarity with other members of the Pth superfamily, with a conserved alpha/beta/alpha sandwich fold. A molecular phylogenetic analysis and a structure database search indicated that SaPth is most similar to its homolog in Streptococcus pyogenes, but it has a different substrate-binding cleft state.

Crystal structure of Staphylococcus aureus peptidyl-tRNA hydrolase at a 2.25 A resolution.,Zhang F, Song Y, Niu L, Teng M, Li X Acta Biochim Biophys Sin (Shanghai). 2015 Dec;47(12):1005-10. doi:, 10.1093/abbs/gmv114. Epub 2015 Oct 26. PMID:26508479^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.