Structural basis of glutamate recognition by a dimeric metabotropic glutamate receptor
- N. Kunishima, Y. Shimada, K. Morikawa
- Biology, ChemistryNature
- 26 October 2000
Three different crystal structures of the extracellular ligand-binding region of mGluR1 are determined—in a complex with glutamate and in two unliganded forms, implying that glutamate binding stabilizes both the ‘active’ dimer and the ’closed’ protomer in dynamic equilibrium.
Structures of the extracellular regions of the group II/III metabotropic glutamate receptors
- T. Muto, D. Tsuchiya, K. Morikawa, H. Jingami
- Biology, ChemistryProceedings of the National Academy of Sciences
- 6 March 2007
A general activation mechanism of the dimeric receptor coupled with both ligand-binding and interprotomer rearrangements is proposed and revealed the lateral interaction between the two cysteine-rich domains, which could stimulate clustering of theDimeric receptors on the cell surface.
Structural and functional studies of MinD ATPase: implications for the molecular recognition of the bacterial cell division apparatus
- I. Hayashi, T. Oyama, K. Morikawa
- Biology, ChemistryEMBO Journal
- 17 April 2001
The results suggest that the residues around the ATP‐binding site are required for the direct interaction with MinC, and that ATP binding and hydrolysis play a role as a molecular switch to control the mechanisms of MinCDE‐dependent bacterial cell division.
CENP-T-W-S-X Forms a Unique Centromeric Chromatin Structure with a Histone-like Fold
- T. Nishino, K. Takeuchi, T. Fukagawa
- Biology, ChemistryCell
- 3 February 2012
Structural views of the ligand-binding cores of a metabotropic glutamate receptor complexed with an antagonist and both glutamate and Gd3+
- D. Tsuchiya, N. Kunishima, N. Kamiya, H. Jingami, K. Morikawa
- Chemistry, BiologyProceedings of the National Academy of Sciences…
- 26 February 2002
The structural comparison between the active and resting dimers suggests that glutamate binding tends to induce domain closing and a small shift of a helix in the dimer interface, and an interprotomer contact including the acidic patch inhibited dimer formation by the two open protomers in the active state.
Acetyl-CoA Synthetase 2, a Mitochondrial Matrix Enzyme Involved in the Oxidation of Acetate*
- T. Fujino, J. Kondo, M. Ishikawa, K. Morikawa, Tokuo T. Yamamoto
- BiologyJournal of Biological Chemistry
- 6 April 2001
Subcellular fractionation revealed that AceCS2 is a mitochondrial matrix enzyme, and acetate incorporation indicated that acetyl-CoAs produced by Ace CS2 are utilized mainly for oxidation.
Domain Architectures and Characterization of an RNA-binding Protein, TLS*
- Y. Iko, T. Kodama, K. Morikawa
- Biology, ChemistryJournal of Biological Chemistry
- 22 October 2004
The domain organization of human TLS is examined by a combined approach using limited proteolysis, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, circular dichroism, inductively coupled plasma atomic emission spectroscopy, and NMR spectroscope to find that the RNA recognition motif (RRM) and zinc finger-like domains exclusively form protease-resistant core structures within the isolated TLS protein fragments.
Structure of the whole cytosolic region of ATP-dependent protease FtsH.
- R. Suno, H. Niwa, D. Tsuchiya, Xiaodong Zhang, Masasuke Yoshida, K. Morikawa
- BiologyMolecules and Cells
- 9 June 2006
Crystal structure of the holliday junction DNA in complex with a single RuvA tetramer.
- M. Ariyoshi, T. Nishino, H. Iwasaki, H. Shinagawa, K. Morikawa
- BiologyProceedings of the National Academy of Sciences…
- 18 July 2000
The solved crystal structure of the Holliday junction bound to a single Escherichia coli RuvA tetramer at 3.1-A resolution revealed an open concave architecture with a four-fold symmetry, which suggests a possible scheme for successive base pair rearrangements, which may account for smooth Holliday Junction movement without segmental unwinding.
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