Potential anti-bacterial drug target: Structural characterization of 3,4-dihydroxy-2-butanone-4-phosphate synthase from Salmonella typhimurium LT2

2010 ◽  
Vol 78 (16) ◽  
pp. 3292-3303 ◽  
Author(s):  
Pankaj Kumar ◽  
Mirage Singh ◽  
Ruchi Gautam ◽  
Subramanian Karthikeyan
Keyword(s):  
Salmonella Typhimurium ◽  
Structural Characterization ◽  
Drug Target ◽  
Phosphate Synthase

Enzymatic and structural characterization of an archaeal thiamin phosphate synthase

2014 ◽  
Vol 1844 (4) ◽  
pp. 803-809 ◽  
Author(s):  
Maria Hayashi ◽  
Kazuya Kobayashi ◽  
Hiroyoshi Esaki ◽  
Hiroyuki Konno ◽  
Kenichi Akaji ◽  
...  
Keyword(s):  
Structural Characterization ◽  
Thiamin Phosphate Synthase ◽  
Phosphate Synthase

scholarly journals Biochemical and Structural Characterization of Selective Allosteric Inhibitors of the Plasmodium falciparum Drug Target, Prolyl-tRNA-synthetase

2016 ◽  
Vol 3 (1) ◽  
pp. 34-44 ◽  
Author(s):  
Stephen Nakazawa Hewitt ◽  
David M. Dranow ◽  
Benjamin G. Horst ◽  
Jan A. Abendroth ◽  
Barbara Forte ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Structural Characterization ◽  
Drug Target ◽  
Trna Synthetase ◽  
Allosteric Inhibitors

scholarly journals Structural characterization of free-state and product-stateMycobacterium tuberculosismethionyl-tRNA synthetase reveals an induced-fit ligand-recognition mechanism

IUCrJ ◽  
2018 ◽  
Vol 5 (4) ◽  
pp. 478-490 ◽  
Author(s):  
Wei Wang ◽  
Bo Qin ◽  
Justyna Aleksandra Wojdyla ◽  
Meitian Wang ◽  
Xiaopan Gao ◽  
...  
Keyword(s):  
Drug Design ◽  
Structural Characterization ◽  
Drug Target ◽  
Multidrug Resistant ◽  
Trna Synthetase ◽  
Free State ◽  
Induced Fit ◽  
Recognition Mechanism ◽  
Methionyl Trna Synthetase

Mycobacterium tuberculosis(MTB) caused 10.4 million cases of tuberculosis and 1.7 million deaths in 2016. The incidence of multidrug-resistant and extensively drug-resistant MTB is becoming an increasing threat to public health and the development of novel anti-MTB drugs is urgently needed. Methionyl-tRNA synthetase (MetRS) is considered to be a valuable drug target. However, structural characterization ofM. tuberculosisMetRS (MtMetRS) was lacking for decades, thus hampering drug design. Here, two high-resolution crystal structures of MtMetRS are reported: the free-state structure (apo form; 1.9 Å resolution) and a structure with the intermediate product methionyl-adenylate (Met-AMP) bound (2.4 Å resolution). It was found that free-state MtMetRS adopts a previously unseen conformation that has never been observed in other MetRS homologues. The pockets for methionine and AMP are not formed in free-state MtMetRS, suggesting that it is in a nonproductive conformation. Combining these findings suggests that MtMetRS employs an induced-fit mechanism in ligand binding. By comparison with the structure of human cytosolic MetRS, additional pockets specific to MtMetRS that could be used for anti-MTB drug design were located.

scholarly journals Structural characterization of inhibitor complexes with checkpoint kinase 2 (Chk2), a drug target for cancer therapy

2011 ◽  
Vol 176 (3) ◽  
pp. 292-301 ◽  
Author(s):  
George T. Lountos ◽  
Andrew G. Jobson ◽  
Joseph E. Tropea ◽  
Christopher R. Self ◽  
Guangtao Zhang ◽  
...  
Keyword(s):  
Cancer Therapy ◽  
Structural Characterization ◽  
Drug Target ◽  
Checkpoint Kinase ◽  
Checkpoint Kinase 2

Structural Characterization of the Enzyme−Substrate, Enzyme−Intermediate, and Enzyme−Product Complexes of Thiamin Phosphate Synthase†,‡

Biochemistry ◽  
2001 ◽  
Vol 40 (34) ◽  
pp. 10103-10114 ◽  
Author(s):  
Diane H. Peapus ◽  
Hsiu-Ju Chiu ◽  
Nino Campobasso ◽  
Jason J. Reddick ◽  
Tadhg P. Begley ◽  
...  
Keyword(s):  
Structural Characterization ◽  
Enzyme Product ◽  
Enzyme Substrate ◽  
Thiamin Phosphate Synthase ◽  
Enzyme Intermediate ◽  
Phosphate Synthase

scholarly journals Biochemical and Structural Characterization of Mycobacterial Aspartyl-tRNA Synthetase AspS, a Promising TB Drug Target

PLoS ONE ◽  
2014 ◽  
Vol 9 (11) ◽  
pp. e113568 ◽  
Author(s):  
Sudagar S. Gurcha ◽  
Veeraraghavan Usha ◽  
Jonathan A. G. Cox ◽  
Klaus Fütterer ◽  
Katherine A. Abrahams ◽  
...  
Keyword(s):  
Structural Characterization ◽  
Drug Target ◽  
Trna Synthetase

scholarly journals Structural characterization of the Salmonella typhimurium LT2 umu operon.

1990 ◽  
Vol 172 (9) ◽  
pp. 4979-4987 ◽  
Author(s):  
S M Thomas ◽  
H M Crowne ◽  
S C Pidsley ◽  
S G Sedgwick
Keyword(s):  
Salmonella Typhimurium ◽  
Structural Characterization

New ultrastructural findings about Borrelia burgdorferi by cryofixation, negative staining, thin sectioning and scanning techniques

1990 ◽  
Vol 48 (3) ◽  
pp. 582-583
Author(s):  
S. F. Hayes ◽  
M. D. Corwin ◽  
T. G. Schwan ◽  
D. W. Dorward ◽  
W. Burgdorfer
Keyword(s):  
Lyme Disease ◽  
Borrelia Burgdorferi ◽  
Structural Characterization ◽  
Negative Staining ◽  
Low Speed ◽  
Thin Sectioning ◽  
Ultrastructural Findings

Characterization of Borrelia burgdorferi strains by means of negative staining EM has become an integral part of many studies related to the biology of the Lyme disease organism. However, relying solely upon negative staining to compare new isolates with prototype B31 or other borreliae is often unsatisfactory. To obtain more satisfactory results, we have relied upon a correlative approach encompassing a variety EM techniques, i.e., scanning for topographical features and cryotomy, negative staining and thin sectioning to provide a more complete structural characterization of B. burgdorferi.For characterization, isolates of B. burgdorferi were cultured in BSK II media from which they were removed by low speed centrifugation. The sedimented borrelia were carefully resuspended in stabilizing buffer so as to preserve their features for scanning and negative staining. Alternatively, others were prepared for conventional thin sectioning and for cryotomy using modified procedures. For thin sectioning, the fixative described by Ito, et al.

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