4YLY

Crystal structure of peptidyl-tRNA hydrolase from a Gram-positive bacterium, staphylococcus aureus at 2.25 angstrom resolution

4YLY の概要

• エントリーDOI: 10.2210/pdb4yly/pdb
• 分子名称: Peptidyl-tRNA hydrolase, GLYCEROL (3 entities in total)
• 機能のキーワード: hydrolase, gram-positive
• 由来する生物種: Staphylococcus aureus
• 細胞内の位置: Cytoplasm: Q6YP15
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 46066.89

構造登録者

Zhang, F.,Song, Y.,Li, X.,Teng, M.K. (登録日: 2015-03-06, 公開日: 2016-01-27, 最終更新日: 2023-11-08)

主引用文献

Zhang, F.,Song, Y.,Niu, L.,Teng, M.,Li, X.
Crystal structure of Staphylococcus aureus peptidyl-tRNA hydrolase at a 2.25 angstrom resolution.
Acta Biochim.Biophys.Sin., 47:1005-1010, 2015

PubMed Abstract: 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.

PubMed: 26508479
DOI: 10.1093/abbs/gmv114

実験手法

X-RAY DIFFRACTION (2.25 Å)