Satoshi Murakami

Summary

Affiliation: Tokyo Institute of Technology
Country: Japan

Publications

  1. doi request reprint Multidrug efflux transporter, AcrB--the pumping mechanism
    Satoshi Murakami
    Department of Life Science, Tokyo Institute of Technology, Nagatsuta, Yokohama, Japan
    Curr Opin Struct Biol 18:459-65. 2008
  2. ncbi request reprint [Structure and reaction mechanism of multi-drug efflux transporter]
    Satoshi Murakami
    Tanpakushitsu Kakusan Koso 52:406-14. 2007
  3. ncbi request reprint Crystal structure of bacterial multidrug efflux transporter AcrB
    Satoshi Murakami
    Department of Cell Membrane Biology, Institute of Scientific and Industrial Research, Osaka University, Ibaraki, Osaka 567 0047, Japan
    Nature 419:587-93. 2002
  4. ncbi request reprint [Crystal structure of bacterial multidrug efflux transporter AcrB]
    Satoshi Murakami
    Tanpakushitsu Kakusan Koso 48:26-32. 2003
  5. ncbi request reprint Extramembrane central pore of multidrug exporter AcrB in Escherichia coli plays an important role in drug transport
    Satoshi Murakami
    Department of Cell Membrane Biology, Institute of Scientific and Industrial Research, Osaka University, Ibaraki, Osaka 567 0047, Japan
    J Biol Chem 279:3743-8. 2004
  6. ncbi request reprint Direct interaction of multidrug efflux transporter AcrB and outer membrane channel TolC detected via site-directed disulfide cross-linking
    Norihisa Tamura
    Department of Cell Membrane Biology, Institute of Scientific and Industrial Research, Osaka University, Ibaraki, Osaka 567 0047, Japan
    Biochemistry 44:11115-21. 2005
  7. ncbi request reprint Processing of membrane protein crystal using ultraviolet laser irradiation
    Hiroshi Kitano
    Department of Electrical Engineering, Graduate School of Engineering, Osaka University, 2 1 Yamadaoka, Suita, Osaka 565 0871, Japan
    J Biosci Bioeng 100:50-3. 2005
  8. ncbi request reprint Multidrug-exporting secondary transporters
    Satoshi Murakami
    Department of Cell Membrane Biology, Institute of Scientific and Industrial Research, Osaka University, 8 1 Mihogaoka, Ibaraki, 567 0047, Osaka, Japan
    Curr Opin Struct Biol 13:443-52. 2003
  9. ncbi request reprint Crystal structures of a multidrug transporter reveal a functionally rotating mechanism
    Satoshi Murakami
    Department of Cell Membrane Biology, Institute of Scientific and Industrial Research, Osaka University, Ibaraki, Osaka 567 0047, Japan
    Nature 443:173-9. 2006
  10. ncbi request reprint Crystal structure of the DsbB-DsbA complex reveals a mechanism of disulfide bond generation
    Kenji Inaba
    Institute for Virus Research, Kyoto University and CREST, Japan Science and Technology Agency, Kyoto 606 8507, Japan
    Cell 127:789-801. 2006

Collaborators

Detail Information

Publications12

  1. doi request reprint Multidrug efflux transporter, AcrB--the pumping mechanism
    Satoshi Murakami
    Department of Life Science, Tokyo Institute of Technology, Nagatsuta, Yokohama, Japan
    Curr Opin Struct Biol 18:459-65. 2008
    ..The structures indicate that drugs are transported by a three-step functional rotation in which substrates undergo ordered binding change...
  2. ncbi request reprint [Structure and reaction mechanism of multi-drug efflux transporter]
    Satoshi Murakami
    Tanpakushitsu Kakusan Koso 52:406-14. 2007
  3. ncbi request reprint Crystal structure of bacterial multidrug efflux transporter AcrB
    Satoshi Murakami
    Department of Cell Membrane Biology, Institute of Scientific and Industrial Research, Osaka University, Ibaraki, Osaka 567 0047, Japan
    Nature 419:587-93. 2002
    ....
  4. ncbi request reprint [Crystal structure of bacterial multidrug efflux transporter AcrB]
    Satoshi Murakami
    Tanpakushitsu Kakusan Koso 48:26-32. 2003
  5. ncbi request reprint Extramembrane central pore of multidrug exporter AcrB in Escherichia coli plays an important role in drug transport
    Satoshi Murakami
    Department of Cell Membrane Biology, Institute of Scientific and Industrial Research, Osaka University, Ibaraki, Osaka 567 0047, Japan
    J Biol Chem 279:3743-8. 2004
    ....
  6. ncbi request reprint Direct interaction of multidrug efflux transporter AcrB and outer membrane channel TolC detected via site-directed disulfide cross-linking
    Norihisa Tamura
    Department of Cell Membrane Biology, Institute of Scientific and Industrial Research, Osaka University, Ibaraki, Osaka 567 0047, Japan
    Biochemistry 44:11115-21. 2005
    ..The cross-linking was not affected by AcrA, the substrate, or a putative proton coupling site mutation...
  7. ncbi request reprint Processing of membrane protein crystal using ultraviolet laser irradiation
    Hiroshi Kitano
    Department of Electrical Engineering, Graduate School of Engineering, Osaka University, 2 1 Yamadaoka, Suita, Osaka 565 0871, Japan
    J Biosci Bioeng 100:50-3. 2005
    ..The results described here indicate that PULSA processing is an effective tool for membrane protein crystals, as well as for soluble protein crystals...
  8. ncbi request reprint Multidrug-exporting secondary transporters
    Satoshi Murakami
    Department of Cell Membrane Biology, Institute of Scientific and Industrial Research, Osaka University, 8 1 Mihogaoka, Ibaraki, 567 0047, Osaka, Japan
    Curr Opin Struct Biol 13:443-52. 2003
    ....
  9. ncbi request reprint Crystal structures of a multidrug transporter reveal a functionally rotating mechanism
    Satoshi Murakami
    Department of Cell Membrane Biology, Institute of Scientific and Industrial Research, Osaka University, Ibaraki, Osaka 567 0047, Japan
    Nature 443:173-9. 2006
    ..The voluminous binding pocket is aromatic and allows multi-site binding. The structures indicate that drugs are exported by a three-step functionally rotating mechanism in which substrates undergo ordered binding change...
  10. ncbi request reprint Crystal structure of the DsbB-DsbA complex reveals a mechanism of disulfide bond generation
    Kenji Inaba
    Institute for Virus Research, Kyoto University and CREST, Japan Science and Technology Agency, Kyoto 606 8507, Japan
    Cell 127:789-801. 2006
    ..We propose that DsbB is converted by its specific substrate, DsbA, to a superoxidizing enzyme, capable of oxidizing this extremely oxidizing oxidase...
  11. ncbi request reprint [Structural basis of xenobiotic recognition by a bacterial xenobiotic exporter]
    Satoshi Murakami
    Institute of Scientific and Industrial Research, Osaka University, Mihogaoka 8 1, Ibaraki, Osaka 567 0047, Japan
    Seikagaku 79:542-9. 2007
  12. ncbi request reprint Solution-stirring method improves crystal quality of human triosephosphate isomerase
    Hiroaki Adachi
    SOSHO Project Crystal Design Project, Osaka University, 2 1 Yamadaoka, Suita, Osaka 565 0871, Japan
    J Biosci Bioeng 101:83-6. 2006
    ..8 A. These results clearly show that the solution-stirring method is valuable and useful for protein crystallization because of its effectiveness and simplicity...