Three-dimensional structures of unligated uridine phosphorylase from Yersinia pseudotuberculosis at 1.4 Å resolution and its complex with an antibacterial drug
作者： VV Balaev , AA Lashkov , AG Gabdulkhakov , MV Dontsova , AS Mironov
DOI: 10.1134/S1063774515040069
关键词: Uridine phosphorylase 、 Yersinia pseudotuberculosis 、 Biochemistry 、 Yersiniosis 、 Trimethoprim 、 Bacterial cell structure 、 Pyrimidine Phosphorylases 、 Uridine 、 Chemistry 、 Bacteria
摘要: Uridine phosphorylases play an essential role in the cellular metabolism of some antibacterial agents. Acute infectious diseases (bubonic plague, yersiniosis, pseudotuberculosis, etc., caused by bacteria genus Yersinia) are treated using both sulfanilamide medicines and antibiotics, including trimethoprim. The action antibiotic on a bacterial cell is determined primarily character its interactions with components, those which not targets (for example, pyrimidine phosphorylases). This type interaction should be taken into account designing drugs. three-dimensional structure uridine phosphorylase from bacterium Yersinia pseudotuberculosis (YptUPh) free active site was for first time X-ray crystallography refined at 1.40 A resolution (DPI = 0.062 A; ID PDB: 4OF4). complex YptUPh bacteriostatic drug trimethoprim studied molecular docking dynamics methods. molecule shown to buffered enzyme YptUPh, resulting decrease efficiency treatment
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Mois Ilia Aroyo, H Wondratschek, International tables for crystallography Kluwer. ,(2002)
W. L. Delano, The PyMOL Molecular Graphics System DeLano Scientific. ,(2002)
J. E. Alouf, J. H. Freer, The comprehensive sourcebook of bacterial protein toxins Academic Press. ,(1999)
Mac Faddin, F Jean, Biochemical tests for identification of medical bacteria Published in <b>2000</b> in Baltimore Md) by Williams and Wilkins. ,(1976)
Thomas Butler, Plague and Other Yersinia Infections ,(1983)
Alexander A. Lashkov, Nadezhda E. Zhukhlistova, Azat H. Gabdoulkhakov, Alexander A. Shtil, Roman G. Efremov, Christian Betzel, Al'bert M. Mikhailov, The X-ray structure of Salmonella typhimurium uridine nucleoside phosphorylase complexed with 2,2'-anhydrouridine, phosphate and potassium ions at 1.86 A resolution. Acta Crystallographica Section D-biological Crystallography. ,vol. 66, pp. 51- 60 ,(2010) , 10.1107/S0907444909044175
Richard A. Friesner, Jay L. Banks, Robert B. Murphy, Thomas A. Halgren, Jasna J. Klicic, Daniel T. Mainz, Matthew P. Repasky, Eric H. Knoll, Mee Shelley, Jason K. Perry, David E. Shaw, Perry Francis, Peter S. Shenkin, Glide: a new approach for rapid, accurate docking and scoring. 1. Method and assessment of docking accuracy. Journal of Medicinal Chemistry. ,vol. 47, pp. 1739- 1749 ,(2004) , 10.1021/JM0306430
Maria Zolotukhina, Irina Ovcharova, Svetlana Eremina, Liubov Errais Lopes, Alexander S Mironov, None, Comparison of the structure and regulation of the udp gene of Vibrio cholerae, Yersinia pseudotuberculosis, Salmonella typhimurium, and Escherichia coli. Research in Microbiology. ,vol. 154, pp. 510- 520 ,(2003) , 10.1016/S0923-2508(03)00125-6
Thomas A. Halgren, Robert B. Murphy, Richard A. Friesner, Hege S. Beard, Leah L. Frye, W. Thomas Pollard, Jay L. Banks, Glide: a new approach for rapid, accurate docking and scoring. 2. Enrichment factors in database screening. Journal of Medicinal Chemistry. ,vol. 47, pp. 1750- 1759 ,(2004) , 10.1021/JM030644S
Maria V. Dontsova, Azat G. Gabdoulkhakov, Olga K. Molchan, Alexandr A. Lashkov, Maria B. Garber, Alexandr S. Mironov, Nadegda E. Zhukhlistova, Ekaterina Yu. Morgunova, Wolfgang Voelter, Christian Betzel, Yang Zhang, Steven E. Ealick, Al'bert M. Mikhailov, Preliminary investigation of the three-dimensional structure of Salmonella typhimurium uridine phosphorylase in the crystalline state. Acta Crystallographica Section F-structural Biology and Crystallization Communications. ,vol. 61, pp. 337- 340 ,(2005) , 10.1107/S1744309105007463