Crystal structure of the tRNA-specific adenosine deaminase from Streptococcus pyogenes

2007 ◽  
Vol 68 (4) ◽  
pp. 1016-1019 ◽  
Author(s):  
Won-Ho Lee ◽  
Young Kwan Kim ◽  
Ki Hyun Nam ◽  
Amit Priyadarshi ◽  
Eun Hye Lee ◽  
...  
2004 ◽  
Vol 55 (2) ◽  
pp. 479-481 ◽  
Author(s):  
Qian Steven Xu ◽  
Dong-Hae Shin ◽  
Ramona Pufan ◽  
Hisao Yokota ◽  
Rosalind Kim ◽  
...  

Structure ◽  
2016 ◽  
Vol 24 (1) ◽  
pp. 70-79 ◽  
Author(s):  
Donghyun Ka ◽  
Hasup Lee ◽  
Yi-Deun Jung ◽  
Kyunggon Kim ◽  
Chaok Seok ◽  
...  

2018 ◽  
Author(s):  
Behnoush Hajian ◽  
Jolanta Krucinska ◽  
Michael Martins ◽  
Narendran G-Dayanan ◽  
Kishore Viswanathan ◽  
...  

ABSTRACTStreptococcus pyogenes, a beta-hemolytic bacterium, causes a wide spectrum of infections in human including pharyngitis, tonsillitis, scarlet fever, rheumatic fever, and necrotizing fasciitis. Streptococcal infections can also exist as co-infection with methicillin resistant Staphylococcus aureus (MRSA). Trimethoprim-sulfamethoxazole (TMP-SMX) combination has been used for treatment of S. pyogenes and MRSA co-infection. However, resistance to TMP, an inhibitor of dihydrofolate reductase enzyme (DHFR), has challenged the efficacy of TMP-SMX combination. We explored the activity of a series of novel DHFR inhibitors against S. pyogenes. This study identified potent inhibitors of DHFR enzyme from S. pyogenes with excellent inhibitory activity against the growth of the live bacteria. We determined, for the first time, the crystal structure of S. pyogenes DHFR which provides structural insights into design and development of antifolate agents against this global pathogen.


2005 ◽  
Vol 280 (16) ◽  
pp. 16002-16008 ◽  
Author(s):  
Mitsuo Kuratani ◽  
Ryohei Ishii ◽  
Yoshitaka Bessho ◽  
Ryuya Fukunaga ◽  
Toru Sengoku ◽  
...  

The bacterial tRNA adenosine deaminase (TadA) generates inosine by deaminating the adenosine residue at the wobble position of tRNAArg-2. This modification is essential for the decoding system. In this study, we determined the crystal structure ofAquifex aeolicusTadA at a 1.8-Å resolution. This is the first structure of a deaminase acting on tRNA.A. aeolicusTadA has an α/β/α three-layered fold and forms a homodimer. TheA. aeolicusTadA dimeric structure is completely different from the tetrameric structure of yeast CDD1, which deaminates mRNA and cytidine, but is similar to the dimeric structure of yeast cytosine deaminase. However, in theA. aeolicusTadA structure, the shapes of the C-terminal helix and the regions between the β4 and β5 strands are quite distinct from those of yeast cytosine deaminase and a large cavity is produced. This cavity contains many conserved amino acid residues that are likely to be involved in either catalysis or tRNA binding. We made a docking model of TadA with the tRNA anticodon stem loop.


2019 ◽  
Vol 667 ◽  
pp. 6-13
Author(s):  
Aritsara Jaruwat ◽  
Pinpunya Riangrungroj ◽  
Sakunrat Ubonprasert ◽  
Udom Sae-ueng ◽  
Buabarn Kuaprasert ◽  
...  

2014 ◽  
Vol 111 (18) ◽  
pp. 6714-6719 ◽  
Author(s):  
B. Trastoy ◽  
J. V. Lomino ◽  
B. G. Pierce ◽  
L. G. Carter ◽  
S. Gunther ◽  
...  

2006 ◽  
Vol 13 (2) ◽  
pp. 153-159 ◽  
Author(s):  
Heather C Losey ◽  
Alexander J Ruthenburg ◽  
Gregory L Verdine

2001 ◽  
Vol 314 (4) ◽  
pp. 789-796 ◽  
Author(s):  
Kazutaka Murayama ◽  
Peter Orth ◽  
Ana B de la Hoz ◽  
Juan C Alonso ◽  
Wolfram Saenger

2009 ◽  
Vol 386 (3) ◽  
pp. 754-772 ◽  
Author(s):  
Todd F. Kagawa ◽  
Maurice R. O'Connell ◽  
Pania Mouat ◽  
Max Paoli ◽  
Paul W. O'Toole ◽  
...  

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