Structure of Francisella tularensis peptidyl-tRNA hydrolase

被引：21
|
作者：
Clarke, Teresa E. [1 ,2 ]
Romanov, Vladimir [1 ,2 ]
Lam, Robert [1 ,2 ]
Gothe, Scott A. [3 ]
Peddi, Srinivasa R. [3 ]
Razumova, Ekaterina B. [2 ]
Lipman, Richard S. A. [3 ]
Branstrom, Arthur A. [3 ]
Chirgadze, Nickolay Y. [1 ,2 ,4 ]
机构：
[1] Ontario Canc Inst, Univ Hlth Network, Div Canc Genom & Prote, Toronto, ON M5G 2C4, Canada
[2] NEXTEX Technol Inc, Toronto, ON M4N 1W6, Canada
[3] PTC Therapeut Inc, S Plainfield, NJ 07080 USA
[4] Univ Toronto, Dept Pharmacol & Toxicol, Toronto, ON M5S 1A8, Canada
来源：
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2011年 / 67卷
关键词：
peptidyl-tRNA hydrolases; Francisella tularensis; CRYSTAL-STRUCTURE; ANGSTROM RESOLUTION; METABOLIC ROLE; PROTEIN; ENZYME;
D O I：
10.1107/S174430911100515X
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
The rational design of novel antibiotics for bacteria involves the identification of inhibitors for enzymes involved in essential biochemical pathways in cells. In this study, the cloning, expression, purification, crystallization and structure of the enzyme peptidyl-tRNA hydrolase from Francisella tularensis, the causative agent of tularemia, was performed. The structure of F. tularensis peptidyl-tRNA hydrolase is comparable to those of other bacterial peptidyl-tRNA hydrolases, with most residues in the active site conserved amongst the family. The resultant reagents, structural data and analyses provide essential information for the structure-based design of novel inhibitors for this class of proteins.
引用
收藏
页码：446 / 449
页数：4
相关论文
共 50 条
  • [21] Expression, purification, and buffer solubility optimization of the putative human peptidyl-tRNA hydrolase PTRHD1
    Burks, Geordan L.
    McFeeters, Hana
    McFeeters, Robert L.
    PROTEIN EXPRESSION AND PURIFICATION, 2016, 126 : 49 - 54
  • [22] Crystal structure of peptidyl-tRNA hydrolase from a Gram-positive bacterium, Streptococcus pyogenes at 2.19 Å resolution shows the closed structure of the substrate-binding cleft
    Singh, Avinash
    Gautam, Lovely
    Sinha, Mau
    Bhushan, Asha
    Kaur, Punit
    Sharma, Sujata
    Singh, T. P.
    FEBS OPEN BIO, 2014, 4 : 915 - 922
  • [23] 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
  • [24] Metapopulation structure for perpetuation of Francisella tularensis tularensis
    Heidi K Goethert
    Benjamin Saviet
    Sam R Telford
    BMC Microbiology, 9
  • [25] The Role of Release Factors in the Hydrolysis of Ester Bond in Peptidyl-tRNA
    Balasanyants, Samson M.
    Aleksandrova, Elena V.
    Polikanov, Yury S.
    BIOCHEMISTRY-MOSCOW, 2021, 86 (09) : 1122 - 1127
  • [26] Unveiling the Druggable Landscape of Bacterial Peptidyl tRNA Hydrolase: Insights into Structure, Function, and Therapeutic Potential
    Mundra, Surbhi
    Kabra, Ashish
    BIOMOLECULES, 2024, 14 (06)
  • [27] Small Molecule Binding, Docking, and Characterization of the Interaction between Pth1 and Peptidyl-tRNA
    Hames, Mary C.
    McFeeters, Hana
    Holloway, W. Blake
    Stanley, Christopher B.
    Urban, Volker S.
    McFeeters, Robert L.
    INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, 2013, 14 (11): : 22741 - 22752
  • [28] The Crystal Structure of Francisella tularensis AcpA
    Felts, Richard
    Tanner, John
    Reilly, Thomas
    ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES, 2005, 61 : C185 - C185
  • [29] Structure of aspartate β-semialdehyde dehydrogenase from Francisella tularensis
    Mank, N. J.
    Pote, S.
    Majorek, K. A.
    Arnette, A. K.
    Klapper, V. G.
    Hurlburt, B. K.
    Chruszcz, M.
    ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 2018, 74 : 14 - 22
  • [30] Large Scale Structural Rearrangement of a Serine Hydrolase from Francisella tularensis Facilitates Catalysis
    Filippova, Ekaterina V.
    Weston, Leigh A.
    Kuhn, Misty L.
    Geissler, Brett
    Gehring, Alexandra M.
    Armoush, Nicola
    Adkins, Chinessa T.
    Minasov, George
    Dubrovska, Ievgeniia
    Shuvalova, Ludmilla
    Winsor, James R.
    Lavis, Luke D.
    Satchell, Karla J. F.
    Becker, Daniel P.
    Anderson, Wayne F.
    Johnson, R. Jeremy
    JOURNAL OF BIOLOGICAL CHEMISTRY, 2013, 288 (15) : 10522 - 10535
12345