Team Leader
Mikako Shirouzu Ph.D.

Laboratory for Protein Functional and Structural Biology

E-mailmikako.shirouzu[at]riken.jp

Please replace [at] with @.

Establishment of a structural analysis technology platform that contributes to "life innovation" such as drug development and medical treatment.

The high-resolution structural information of proteins related to diseases shall increasingly become important for drug development leading to future individualized medicine. We plan to establish a structural analysis technology platform to contribute to "Life innovation" such as drug discovery as well as development of methods for the sample preparation of challenging proteins including membrane proteins/biomolecular complexes and for the structural analysis by cryo-electron microscopy (cryo-EM). The 3D-structural information will be used for in-silico screening/design of chemical compounds and for dynamic structural analysis toward simulation research of cell function.

cryo-EM (FEI Tecnai Arctica)

Research Theme

Analysis of developmental process using theoretical cell models
Study of evolutionary dynamics of microorganisms by comprehensive phenotypic/genetic analysis
Development of algorithm for high-resolution comprehensive phenotypic/genetic analysis

Selected Publications

Yamagata A, Murata Y, Namba K, et al.
Uptake mechanism of iron-phytosiderophore from the soil based on the structure of yellow stripe transporter.
Nature Communications 13, 7180 (2022) doi: 10.1038/s41467-022-34930-1

Ehara H, Kujirai T, Shirouzu M, et al.
Structural basis of nucleosome disassembly and reassembly by RNAPII elongation complex with FACT.
Science 377(6611), eabp9466 (2022) doi: 10.1126/science.abp9466

Nakamura H, Hisano T, Rahman MM, et al.
Structural basis for heme detoxification by an ATP-binding cassette-type efflux pump in gram-positive pathogenic bacteria.
Proceedings of the National Academy of Sciences of the United States of America 119(27), e2123385119 (2022) doi: 10.1073/pnas.2123385119

Park JH, Iwamoto M, Yun JH, et al.
Structural insights into the HBV receptor and bile acid transporter NTCP.
Nature 606(7916), 1027-1031 (2022) doi: 10.1038/s41586-022-04857-0

Cao P, Bracun L, Yamagata A, et al.
Structural basis for the assembly and quinone transport mechanisms of the dimeric photosynthetic RC-LH1 supercomplex.
Nature Communications 13, 1977 (2022) doi: 10.1038/s41467-022-29563-3

Hosaka T, Nomura T, Kubo M, et al.
Conformational alterations in unidirectional ion transport of a light-driven chloride pump revealed using X-ray free electron lasers.
Proceedings of the National Academy of Sciences of the United States of America 119(9), e2117433119 (2022) doi: 10.1073/pnas.2117433119

Nakagawa Y, Shen HC, Komi Y, et al.
Amyloid conformation-dependent disaggregation in a reconstituted yeast prion system.
Nature Chemical Biology 18(3), 321-331 (2022) doi: 10.1038/s41589-021-00951-y

Shimizu K, Iyoda T, Sanpei A, et al.
Identification of TCR repertoires in functionally competent cytotoxic T cells cross-reactive to SARS-CoV-2.
Communications Biology 4, 1365 (2021) doi: 10.1038/s42003-021-02885-6

Kasahara K, Re S, Nawrocki G, et al.
Reduced Efficacy of a Src Kinase Inhibitor in Crowded Protein Solution.
Nature Communications 12, 4099 (2021) doi: 10.1038/s41467-021-24349-5

Kukimoto-Niino M, Katsura K, Kaushik R, et al.
Cryo-EM structure of the human ELMO1-DOCK5-Rac1 complex.
Science Advances 7(30), eabg3147 (2021) doi: 10.1126/sciadv.abg3147