Crystal structure of Staphylococcus aureus peptidyl-tRNA hydrolase at a 2.25 Å resolution

被引：10
作者：
Zhang, Fan [1 ,2 ]
Song, Yang [1 ,2 ]
Niu, Liwen [1 ,2 ]
Teng, Maikun [1 ,2 ]
Li, Xu [1 ,2 ]
机构：
[1] Univ Sci & Technol China, Sch Life Sci, Innovat Ctr Cell Signaling Network, Hefei Natl Lab Phys Sci Microscale, Hefei 230026, Peoples R China
[2] Chinese Acad Sci, Hefei Sci Ctr, Key Lab Struct Biol, Hefei 230026, Peoples R China
来源：
ACTA BIOCHIMICA ET BIOPHYSICA SINICA | 2015年 / 47卷 / 12期
关键词：
peptidyl-tRNA hydrolase; Staphylococcus aureus; SaPth; crystal structure; substrate-binding cleft; CRYSTALLOGRAPHIC STRUCTURE DETERMINATION; RECOMBINANT PRODUCTION; ENZYMATIC-HYDROLYSIS; PROTEIN-SYNTHESIS; METABOLIC ROLE; CRYSTALLIZATION; INHIBITION; RIBOSOMES; REVEALS; SITE;
D O I：
10.1093/abbs/gmv114
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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 angstrom 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.
引用
收藏
页码：1005 / 1010
页数：6
相关论文
共 50 条
  • [31] Peptidyl-tRNA hydrolase is the nascent chain release factor in bacterial ribosome-associated quality control
    Svetlov, Maxim S.
    Dunand, Clemence F.
    Nakamoto, Jose A.
    Atkinson, Gemma C.
    Safdari, Haaris A.
    Wilson, Daniel N.
    Vazquez-Laslop, Nora
    Mankin, Alexander S.
    MOLECULAR CELL, 2024, 84 (04) : 715 - 726.e5
  • [32] The growth defect in Escherichia coli deficient in peptidyl-tRNA hydrolase is due to starvation for Lys-tRNA(Lys)
    HeurgueHamard, V
    Mora, L
    Guarneros, G
    Buckingham, RH
    EMBO JOURNAL, 1996, 15 (11) : 2826 - 2833
  • [33] Recombinant production, crystallization and X-ray crystallographic structure determination of peptidyl-tRNA hydrolase from Salmonella typhimurium
    Vandavasi, Venugopal
    Taylor-Creel, Kasey
    McFeeters, Robert L.
    Coates, Leighton
    McFeeters, Hana
    ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 2014, 70 : 872 - 877
  • [34] Natural Product Inhibition and Enzyme Kinetics Related to Phylogenetic Characterization for Bacterial Peptidyl-tRNA Hydrolase 1
    Strange, D. Scott
    Gaffin, Steven S.
    Holloway, W. Blake
    Kinsella, Meredyth D.
    Wisotsky, Jacob N.
    McFeeters, Hana
    McFeeters, Robert L.
    MOLECULES, 2021, 26 (08):
  • [35] A functional peptidyl-tRNA hydrolase, ICT1, has been recruited into the human mitochondrial ribosome
    Richter, Ricarda
    Rorbach, Joanna
    Pajak, Aleksandra
    Smith, Paul M.
    Wessels, Hans J.
    Huynen, Martijn A.
    Smeitink, Jan A.
    Lightowlers, Robert N.
    Chrzanowska-Lightowlers, Zofia M.
    EMBO JOURNAL, 2010, 29 (06) : 1116 - 1125
  • [36] Peptidyl-tRNA Hydrolase Screening Combined with Molecular Docking Reveals the Antibiotic Potential of Syzygium johnsonii Bark Extract
    Harris, Sarah M.
    McFeeters, Hana
    Ogungbe, Ifedayo V.
    Cruz-Vera, Luis R.
    Setzer, William N.
    Jackes, Betsy R.
    McFeeters, Robert L.
    NATURAL PRODUCT COMMUNICATIONS, 2011, 6 (10) : 1421 - 1424
  • [37] Crystal structure of Staphylococcus aureus tyrosyl-tRNA synthetase in complex with a class of potent and specific inhibitors
    Qiu, XY
    Janson, CA
    Smith, WW
    Green, SM
    McDevitt, P
    Johanson, K
    Carter, P
    Hibbs, M
    Lewis, C
    Chalker, A
    Fosberry, A
    Lalonde, J
    Berge, J
    Brown, P
    Houge-Frydrych, CSV
    Jarvest, RL
    PROTEIN SCIENCE, 2001, 10 (10) : 2008 - 2016
  • [38] Crystal structure of exfoliative toxin D from Staphylococcus aureus
    Sato, Shu
    Ragab, Rokaia F.
    Guo, Xu
    Elfadadny, Ahmed
    Kozono, Takuma
    Nishikawa, Atsushi
    Nishifuji, Koji
    Tonozuka, Takashi
    BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2024, 733
  • [39] Crystal structure of FtsA from Staphylococcus aureus
    Fujita, Junso
    Maeda, Yoko
    Nagao, Chioko
    Tsuchiya, Yuko
    Miyazaki, Yuma
    Hirose, Mika
    Mizohata, Eiichi
    Matsumoto, Yoshimi
    Inoue, Tsuyoshi
    Mizuguchi, Kenji
    Matsumura, Hiroyoshi
    FEBS LETTERS, 2014, 588 (10) : 1879 - 1885
  • [40] Crystal Structure of the Metallo- Endoribonuclease YbeY from Staphylococcus aureus
    Lee, Jinwook
    Jo, Inseong
    Kwon, Ae-Ran
    Ha, Nam-Chul
    JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY, 2023, 33 (01) : 28 - 34
12345