Research Topics
Species | Masayoshi NakasakoSummaryAffiliation: Keio University Country: Japan Publications
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Detail Information
Publications
Structural basis of the LOV1 dimerization of Arabidopsis phototropins 1 and 2Masayoshi Nakasako
Department of Physics, Faculty of Science and Technology, Keio University, 3 14 1 Hiyoshi, Kohoku Ku, Kanagawa 223 8522, Japan
J Mol Biol 381:718-33. 2008..The present results also provide clues to understanding structural basis in dimeric interactions of Per-ARNT-Sim protein modules in cellular signaling...
Crystallization and preliminary X-ray diffraction analysis [correction of anaylsis] of the LOV1 domains of phototropin 1 and 2 from Arabidopsis thalianaMasayoshi Nakasako
Department of Physics, Faculty of Science and Technology, Keio University, 3 14 1 Hiyoshi, Kohoku Ku, Kanagawa 223 8522, Japan
Acta Crystallogr Sect F Struct Biol Cryst Commun 64:617-21. 2008..5, b = 66.5, c = 56.7 A, beta = 92.4 degrees , and diffracted X-rays to beyond 2.0 A resolution. In both crystals, two LOV1 domains occupied the crystallographic asymmetric unit...
Conformational dynamics of complementarity-determining region H3 of an anti-dansyl Fv fragment in the presence of its haptenMasayoshi Nakasako
Department of Physics, Faculty of Science and Technology, Keio University, 3 14 1 Hiyoshi, Kohoku Ku, Yokohama, Kanagawa 223 8522, Japan
J Mol Biol 351:627-40. 2005..The conformational dynamics of H3 in recognizing and binding the hapten molecule are discussed on the basis of the structural information from the present and previous studies...
Quaternary structure of LOV-domain containing polypeptide of Arabidopsis FKF1 proteinMasayoshi Nakasako
Department of Physics, Faculty of Science and Technology, Keio University, 3 14 1 Hiyoshi, Kohoku Ku, Kanagawa 223 8522, Japan
FEBS Lett 579:1067-71. 2005..Based on the homologies in the amino-acid sequences and the scattering profiles, these results are discussed in connection with the structures and function of LOV domains of phototropin...
Light-induced global structural changes in phytochrome A regulating photomorphogenesis in plantsMasayoshi Nakasako
Department of Physics, Faculty of Science and Technology, Keio University, 3 14 1 Hiyoshi, Kohoku Ku, Kanagawa 223 8522, Japan
FEBS J 272:603-12. 2005..Red-light-induced structural changes in Pfr were reversible, mostly due to thermal relaxation processes...
Light-induced structural changes of LOV domain-containing polypeptides from Arabidopsis phototropin 1 and 2 studied by small-angle X-ray scatteringMasayoshi Nakasako
Department of Physics, Faculty of Science and Technology, Keio University, 3 14 1, Hiyoshi, Kohoku Ku, Kanagawa 223 8522, Japan
Biochemistry 43:14881-90. 2004..On the basis of the results, the interdomain interactions in phototropin are discussed...
Water-protein interactions from high-resolution protein crystallographyMasayoshi Nakasako
Department of Physics, Faculty of Science and Technology, Keio University, 3 14 1 Hiyoshi, Kohoku Ku, Yokohama, Kanagawa 223 8522, Japan
Philos Trans R Soc Lond B Biol Sci 359:1191-204; discussion 1204-6. 2004....
Redox-dependent domain rearrangement of protein disulfide isomerase from a thermophilic fungusMasayoshi Nakasako
Department of Physics, Faculty of Science and Technology, Keio University, 3 14 1 Hiyoshi, Kouho ku, Yokohama 223 8522, Japan
Biochemistry 49:6953-62. 2010..On the basis of the results presented here, we propose a mechanism explaining the observed redox-dependent conformational and solvation changes of PDI...
Crystallization and preliminary X-ray diffraction experiments of arylmalonate decarboxylase from Alcaligenes bronchisepticusMasayoshi Nakasako
Department of Physics, Faculty of Science and Technology, Keio University, 3 14 1 Hiyoshi, Kohoku Ku, Kanagawa 223 8522, Japan
Acta Crystallogr Sect F Struct Biol Cryst Commun 64:610-3. 2008..Small-angle X-ray scattering revealed that the enzyme exists as a monomer in solution. Thus, the assembly of molecules in the asymmetric unit was likely to have been induced during the crystallization process...
Light-induced movement of the LOV2 domain in an Asp720Asn mutant LOV2-kinase fragment of Arabidopsis phototropin 2Yuki Takayama
Department of Physics, Faculty of Science and Technology, Keio University, 3 14 1Hiyoshi, Kohoku Ku, Kanagawa 223 8522, Japan
Biochemistry 50:1174-83. 2011....
Structural basis for inverting the enantioselectivity of arylmalonate decarboxylase revealed by the structural analysis of the Gly74Cys/Cys188Ser mutant in the liganded formRika Obata
Department of Physics, Faculty of Science and Technology, Keio University, 3 14 1 Hiyoshi, Kohoku Ku, Yokohama, Kanagawa 223 8522, Japan
Biochemistry 49:1963-9. 2010..These results may provide an effective strategy for the rational design to invert the enantioselectivity of enzymes...
Crystal structures of blasticidin S deaminase (BSD): implications for dynamic properties of catalytic zincTakashi Kumasaka
Department of Life Science, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama, Kanagawa 226 8501, Japan
J Biol Chem 282:37103-11. 2007....
Prediction of hydration structures around hydrophilic surfaces of proteins by using the empirical hydration distribution functions from a database analysisDaisuke Matsuoka
Department of Physics, Faculty of Science and Technology, Keio University, 3 14 1 Hiyoshi, Kohoku Ku, Yokohama, Kanagawa 223 8522, Japan
J Phys Chem B 114:4652-63. 2010..In addition, it will be used to predict hydration structures of proteins available at resolutions insufficient to identify water molecules...
Humidity-controlled preparation of frozen-hydrated biological samples for cryogenic coherent x-ray diffraction microscopyYuki Takayama
Department of Physics, Faculty of Science and Technology, Keio University, 3 14 1 Hiyoshi, Kanagawa 223 8522, Japan
Rev Sci Instrum 83:054301. 2012..Taking the performance of the system and the quality of the sample, the system was suitable to prepare frozen-hydrated biological samples for cryogenic CXDM experiments...
Enzymatic characterization of scytalone dehydratase Val75Met variant found in melanin biosynthesis dehydratase inhibitor (MBI-D) resistant strains of the rice blast fungusNaoki Yamada
Department of Physics, Faculty of Science and Technology, Keio University, Yokohama, Kanagawa, Japan
Biosci Biotechnol Biochem 68:615-21. 2004..Based on the results, here we propose possible mechanisms of the carpropamid-resistance of the variant enzyme in retaining the normal enzymatic activity...
A few low-frequency normal modes predominantly contribute to conformational responses of hen egg white lysozyme in the tetragonal crystal to variations of molecular packing controlled by environmental humidityYuki Takayama
Department of Physics, Faculty of Science and Technology, Keio University, 3 14 1 Hiyoshi, Kanagawa 223 8522, Japan
Biophys Chem 159:237-46. 2011..These findings suggest that humidity-controlled X-ray crystallography is an effective tool to investigate the responses of inherent intramolecular motions of proteins to external perturbations...
Probability distributions of hydration water molecules around polar protein atoms obtained by a database analysisDaisuke Matsuoka
Department of Physics, Faculty of Science and Technology, Keio University, Yokohama, Kanagawa 223 8522, Japan
J Phys Chem B 113:11274-92. 2009..These probability distributions are probably one of fundamental data to better understand the roles of hydration water molecules in the folding process and the stability of proteins in solution...
Application of a real-space three-dimensional image reconstruction method in the structural analysis of noncrystalline biological macromolecules enveloped by water in coherent x-ray diffraction microscopyWataru Kodama
Department of Physics, Faculty of Science and Technology, Keio University, 3 14 1 Hiyoshi, Kohoku Ku, Yokohama, Kanagawa 223 8522, Japan
Phys Rev E Stat Nonlin Soft Matter Phys 84:021902. 2011..In particular, we examined the influence of Poisson noise in diffraction patterns on the reconstructed three-dimensional electron density in the proposed protocol...
Hydration structure of human lysozyme investigated by molecular dynamics simulation and cryogenic X-ray crystal structure analyses: on the correlation between crystal water sites, solvent density, and solvent dipoleJunichi Higo
Laboratory of Bioinformatics, School of Life Science, Tokyo University of Pharmacy and Life Science and BIRD, JST Japan Science and Technology Corporation, 1432 1 Horinouchi, Hachioji, Tokyo, 192 0392, Japan
J Comput Chem 23:1323-36. 2002..The present work may provide a new approach combining computational and the experimental studies to understand protein hydration...
Roles of hydration water molecules in molecular packing of the killer toxin from Pichia farinosa in its crystalline state investigated by cryogenic X-ray crystallographyMasayoshi Nakasako
Precursory Research for Embryonic Science and Technology, Japan Science and Technology Corporation and Institute of Molecular and Cellular Biosciences, The University of Tokyo, Yayoi, Bunkyo ku, Tokyo 113 0032, Japan
Biophys Chem 95:211-25. 2002..The present analysis may provide a way to analyze the crystal contact and molecular recognition in macromolecules in aqueous solution...
Nonlinear temperature dependence of the crystal structure of lysozyme: correlation between coordinate shifts and thermal factorsYasumasa Joti
Department of Science, Kyoto University, Kitashirakawa, Sakyo-ku, Japan
Acta Crystallogr D Biol Crystallogr 58:1421-32. 2002..Possible causes for the dynamic transition are discussed with respect to the crystal packing and physicochemical properties of crystalline water...
Crystallization of scytalone dehydratase F162A mutant in the unligated state and a preliminary X-ray diffraction study at 37 KTakayuki Motoyama
RIKEN (The Institute of Physical and Chemical Research, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan
Acta Crystallogr D Biol Crystallogr 58:148-50. 2002..62 A, beta = 120.02 degrees at 37 K. The calculated V(M) value was acceptable when a trimer of the mutant enzyme occupied a crystallographic asymmetric unit. The resolution limit was extended to 1.45 A at BL41XU of SPring-8 at 37 K...
