Open AccessCrystal structure of <italic>Staphylococcus aureus</italic> peptidyl-tRNA hydrolase at a 2.25 Å resolution
Author(s) -
Fan Zhang,
Yang Song,
Liwen Niu,
Maikun Teng,
Li Xu
Publication year - 2015
Publication title -
acta biochimica et biophysica sinica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.771
H-Index - 57
eISSN - 1745-7270
pISSN - 1672-9145
DOI - 10.1093/abbs/gmv114
Subject(s) - hydrolase , transfer rna , chemistry , structural similarity , enzyme , staphylococcus aureus , bacteria , biology , biochemistry , genetics , rna , gene
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 Å resolution. The SaPth structure exhibits significant structural similarity with other members of the Pth superfamily, with a conserved α/β/α 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.