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Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution
Comparison with a low-resolution electron density map of the enzyme in the absence of calcium and with biochemical data suggests that large domain movements take place during active transport.
Crystal structure of the calcium pump of sarcoplasmic reticulum at
Structural basis of the LOV1 dimerization of Arabidopsis phototropins 1 and 2.
Structure of a thermophilic F1‐ATPase inhibited by an ε‐subunit: deeper insight into the ε‐inhibition mechanism
- Y. Shirakihara, A. Shiratori, Hiromi Tanikawa, M. Nakasako, Masasuke Yoshida, Toshiharu Suzuki
- Chemistry, BiologyThe FEBS journal
- 1 August 2015
F1‐ATPase (F1) is the catalytic sector in FoF1‐ATP synthase that is responsible for ATP production in living cells. In catalysis, its three catalytic β‐subunits undergo nucleotide occupancy‐dependent…
Novel non-heme iron center of nitrile hydratase with a claw setting of oxygen atoms
The crystal structure at 1.7 Å resolution and mass spectrometry revealed the structure of the non-heme iron catalytic center in the nitrosylated state, likely to enable the photo-regulation of NHase and will provide an excellent model for designing photo-controllable chelate complexes and, ultimately, proteins.
Water-protein interactions from high-resolution protein crystallography.
- M. Nakasako
- ChemistryPhilosophical transactions of the Royal Society…
- 29 August 2004
Cryogenic X-ray crystallography method enabled a much clearer visualization of definite hydration sites on the protein surface than at ambient temperature and may have profound implications in the understanding of the physico-chemical principles governing the dynamics of proteins in an aqueous environment.
Crystallographic characterization by X‐ray diffraction of the M‐intermediate from the photo‐cycle of bacteriorhodopsin at room temperature
Large-scale networks of hydration water molecules around bovine beta-trypsin revealed by cryogenic X-ray crystal structure analysis.
- M. Nakasako
- ChemistryJournal of molecular biology
- 11 June 1999
The hydration structure of bovine beta-trypsin was investigated in cryogenic X-ray diffraction experiments and showed that the negatively charged active site of trypsin tended to be easily exposed to bulk solvent.
Detailed characterization of the cooperative mechanism of Ca(2+) binding and catalytic activation in the Ca(2+) transport (SERCA) ATPase.
Expression of heterologous SERCA1a ATPase in Cos-1 cells was optimized to yield levels that account for 10-15% of the microsomal protein, as revealed by protein staining on electrophoretic gels, which significantly improved the characterization of mutants.