4YLY

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

Summary for 4YLY

• Entry DOI: 10.2210/pdb4yly/pdb
• Descriptor: Peptidyl-tRNA hydrolase, GLYCEROL (3 entities in total)
• Functional Keywords: hydrolase, gram-positive
• Biological source: Staphylococcus aureus
• Cellular location: Cytoplasm: Q6YP15
• Total number of polymer chains: 2
• Total formula weight: 46066.89

Authors

Zhang, F.,Song, Y.,Li, X.,Teng, M.K. (deposition date: 2015-03-06, release date: 2016-01-27, Last modification date: 2023-11-08)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.25 Å)