Zobrazeno 1 - 10
of 24
pro vyhledávání: '"Ludmila Reshetnikova"'
Autor:
Ludmila Reshetnikova, Andrew G. Szent-Györgyi, Howard Robinson, Carolyn Cohen, Elizabeth O'Neall-Hennessey, V. S. Senthil Kumar
Publikováno v:
Acta Crystallographica Section F Structural Biology and Crystallization Communications. 69:248-252
All muscle-based movement is dependent upon carefully choreographed interactions between the two major muscle components, myosin and actin. Regulation of vertebrate smooth and molluscan muscle contraction is myosin based (both are in the myosin II cl
Autor:
Andrew G. Szent-Györgyi, Elizabeth O'Neall-Hennessey, Ludmila Reshetnikova, Howard Robinson, V. S. Senthil Kumar, Michelle Nguyen-McCarty, Carolyn Cohen, Jerry H. Brown
Publikováno v:
Proceedings of the National Academy of Sciences. 108:114-119
We have determined the 2.3-Å-resolution crystal structure of a myosin light chain domain, corresponding to one type found in sea scallop catch (“smooth”) muscle. This structure reveals hinges that may function in the “on” and “off” stat
Publikováno v:
Journal of Molecular Biology. 287:555-568
The crystal structures of Thermus thermophilus phenylalanyl-tRNA synthetase (PheRS) complexed with phenylalanine and phenylalaninyl-adenylate (PheOH-AMP), the synthetic analogue of phenylalanyl-adenylate, have been determined at 2.7A and 2.5A resolut
Autor:
Jens Nyborg, Ole Steen Kristensen, Poul Nissen, Gunhild E. Siboska, Søren Thirup, Ludmila Reshetnikova
Publikováno v:
Aarhus University
Kristensen, O, Reshetnikova, L, Nissen, P, Siboska, G, Thirup, S & Nyborg, J 1996, ' Isolation, crystallization and X-ray analysis of the quaternary complex of Phe-tRNA(Phe), EF-Tu, a GTP analog and kirromycin ', F E B S Letters, vol. 399, no. 1-2, pp. 59-62 .
Kristensen, O, Reshetnikova, L, Nissen, P, Siboska, G, Thirup, S & Nyborg, J 1996, ' Isolation, crystallization and X-ray analysis of the quaternary complex of Phe-tRNA(Phe), EF-Tu, a GTP analog and kirromycin ', F E B S Letters, vol. 399, no. 1-2, pp. 59-62 .
Udgivelsesdato: 1996-Dec-9 Kirromycin inhibits bacterial protein synthesis by acting on elongation factor Tu (EF-Tu). Complexes of the antibiotic, Phe-tRNA(Phe), the guanosine triphosphate analog GDPNP, and mesophilic (Escherichia coli), as well as t
Autor:
Alexander Wlodawer, Alla Gustchina, Ludmila Reshetnikova, Jacek Lubkowski, Alexander Zdanov, Kwan Y. Hui, Eddie L. Angleton, William G. Farmerie, Maureen M. Goodenow, Deepa Bhatt, Li Zhang, Ben M. Dunn
Publikováno v:
Nature Structural & Molecular Biology. 2:480-488
The crystal structure of a recombinant form of the proteinase encoded by the feline immunodeficiency virus (FIV PR) has been solved at 2 A resolution and refined to an R-factor of 0.148. The refined structure includes a peptidomimetic, statine-based
Autor:
Harald Berchtold, Christian O. A. Reiser, Rolf Hilgenfeld, Ludmila Reshetnikova, Mathias Sprinzl, Norbert K. Schirmer
Publikováno v:
Nature. 365:126-132
The crystal structure of intact elongation factor Tu (EF-Tu) from Thermus thermophilus has been determined and refined at an effective resolution of 1.7 A, with incorporation of data extending to 1.45 A. The effector region, including interaction sit
Autor:
Mark Safro, Dino Moras, Maia Chernaya, Ludmila Reshetnikova, Jean-Cloud Thierry, Marc Delarue, Olga I. Lavrik, V.N. Ankilova
Publikováno v:
European Journal of Biochemistry. 208:411-417
The three-dimensional structure of the heterodimeric alpha 2 beta 2 enzyme phenylalanyl-tRNA synthetase from Thermus thermophilus HB8 has been determined by X-ray crystallography, using the multiple-isomorphous-replacement method at 0.6 nm resolution
Publikováno v:
Journal of molecular biology. 319(3)
Shikimate kinase (SK) and other enzymes in the shikimate pathway are potential targets for developing non-toxic antimicrobial agents, herbicides, and anti-parasite drugs, because the pathway is essential in the above species but is absent from mammal
Autor:
Mark Safro, Ludmila Reshetnikova, Svetlana N. Khodyreva, Olga I. Lavrik, V.N. Ankilova, F. Frolow
Publikováno v:
Journal of Molecular Biology. 231:927-929
Phenylalanyl-tRNA synthetase (EC 6.1.1.20) from the extreme thermophile Thermus thermophilus HB8 has been crystallized with its cognate tRNA. Compared with the native crystals, the crystals of the complex are more stable to radiation damage and diffr
Publikováno v:
Acta crystallographica. Section D, Biological crystallography. 57(Pt 12)
Shikimate kinase (SK) from Mycobacterium tuberculosis (Mt) was overexpressed in Escherichia coli, purified and cocrystallized with MgADP in hanging drops using the vapor-diffusion procedure with PEG 4000 and 2-propanol as precipitants at pH 7.5. The