scholarly journals Identification of the csp gene and molecular modelling of the CspA-like protein from Antarctic soil-dwelling psychrotrophic bacterium Psychrobacter sp. B6.

2009 ◽  
Vol 56 (1) ◽  
Author(s):  
Agnieszka Kaufman-Szymczyk ◽  
Arkadiusz Wojtasik ◽  
Paweł Parniewski ◽  
Aneta Białkowska ◽  
Karolina Tkaczuk ◽  
...  

We cloned and sequenced the cspA-like gene from a psychrotrophic Antarctic soil-dwelling bacterial strain Psychrobacter sp. B6. The gene is 213 bp long and shows 99% and 98% sequence identity with the Psychrobacter cryohalolentis K5 gene encoding a cold-shock DNA-binding domain protein and the Psychrobacter arcticus transcriptional regulator-CspA gene, respectively. The protein encoded by the Psychrobacter sp. B6 cspA-like gene shows 100% identity with the two proteins mentioned above, and also 61% sequence identity with CspB from Bacillus subtilis and Csp from Bacillus caldolyticus, and 56% - with Escherichia coli CspA protein. A three-dimensional model of the CspA-like protein from Psychrobacter sp. B6 was generated based on three known structures of cold shock proteins: the crystal structure of the major cold shock protein from Escherichia coli (CspA), the NMR structure of the latter protein, and the NMR structure of Csp from Thermotoga maritima. The deduced structure of the CspA-like protein from Psychrobacter sp. B6 was found to be very similar to these known structures of Csp-like proteins.

2001 ◽  
Vol 268 (9) ◽  
pp. 2527-2539 ◽  
Author(s):  
Werner Kremer ◽  
Benjamin Schuler ◽  
Stefan Harrieder ◽  
Matthias Geyer ◽  
Wolfram Gronwald ◽  
...  

2015 ◽  
Vol 112 ◽  
pp. 15-20 ◽  
Author(s):  
Antje Lindae ◽  
Raphael J. Eberle ◽  
Icaro P. Caruso ◽  
Monika A. Coronado ◽  
Fabio R. de Moraes ◽  
...  

2010 ◽  
Vol 402 (4) ◽  
pp. 693-698 ◽  
Author(s):  
Gabriella D’Auria ◽  
Carla Esposito ◽  
Lucia Falcigno ◽  
Luisa Calvanese ◽  
Emanuela Iaccarino ◽  
...  

1990 ◽  
Vol 87 (1) ◽  
pp. 283-287 ◽  
Author(s):  
J. Goldstein ◽  
N. S. Pollitt ◽  
M. Inouye

2003 ◽  
Vol 327 (2) ◽  
pp. 521-536 ◽  
Author(s):  
Yuanpeng Janet Huang ◽  
G.V.T. Swapna ◽  
P.K. Rajan ◽  
Haiping Ke ◽  
Bing Xia ◽  
...  

2005 ◽  
Vol 393 (2) ◽  
pp. 503-511 ◽  
Author(s):  
Sergey A. Shiryaev ◽  
Boris I. Ratnikov ◽  
Alexei V. Chekanov ◽  
Sergey Sikora ◽  
Dmitri V. Rozanov ◽  
...  

Mosquito-borne WNV (West Nile virus) is an emerging global threat. The NS3 proteinase, which is essential for the proteolytic processing of the viral polyprotein precursor, is a promising drug target. We have isolated and biochemically characterized the recombinant, highly active NS3 proteinase. We have determined that the NS3 proteinase functions in a manner that is distantly similar to furin in cleaving the peptide and protein substrates. We determined that aprotinin and D-arginine-based 9–12-mer peptides are potent inhibitors of WNV NS3 with Ki values of 26 nM and 1 nM respectively. Consistent with the essential role of NS3 activity in the life cycle of WNV and with the sensitivity of NS3 activity to the D-arginine-based peptides, we showed that nona-D-Arg-NH2 reduced WNV infection in primary neurons. We have also shown that myelin basic protein, a deficiency of which is linked to neurological abnormalities of the brain, is sensitive to NS3 proteolysis in vitro and therefore this protein represents a convenient test substrate for the studies of NS3. A three-dimensional model of WNV NS3 that we created may provide a structural guidance and a rationale for the subsequent design of fine-tuned inhibitors. Overall, our findings represent a foundation for in-depth mechanistic and structural studies as well as for the design of novel and efficient inhibitors of WNV NS3.


1991 ◽  
Vol 221 (1) ◽  
pp. 293-308 ◽  
Author(s):  
Christine Brunel ◽  
Pascale Romby ◽  
Eric Westhof ◽  
Chantal Ehresmann ◽  
Bernard Ehresmann

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