Journal Article

Crystal structure of <i>Staphylococcus aureus</i> peptidyl-tRNA hydrolase at a 2.25 Å resolution

Fan Zhang, Yang Song, Liwen Niu, Maikun Teng and Xu Li

in Acta Biochimica et Biophysica Sinica

Published on behalf of Institute of Biochemistry and Cell Biology, SIBS, CAS

Volume 47, issue 12, pages 1005-1010
Published in print December 2015 | ISSN: 1672-9145
Published online October 2015 | e-ISSN: 1745-7270 | DOI: https://dx.doi.org/10.1093/abbs/gmv114
Crystal structure of Staphylococcus aureus peptidyl-tRNA hydrolase at a 2.25 Å resolution

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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.

Keywords: peptidyl-tRNA hydrolase; Staphylococcus aureus; SaPth; crystal structure; substrate-binding cleft

Journal Article.  4165 words.  Illustrated.

Subjects: Biochemistry

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