Sahoko Tomida
Nagoya Institute of Technology
11 Papers
19 Citations
Sahoko Tomida is an academic researcher from Nagoya Institute of Technology. The author has contributed to research in topics: Rhodopsin & Bacteriorhodopsin. The author has an hindex of 7, co-authored 9 publications.
Chat about Author
Papers
Crystal structure of heliorhodopsin.
Wataru Shihoya,Keiichi Inoue,Manish Singh,Masae Konno,Shoko Hososhima,Keitaro Yamashita,Kento Ikeda,Akimitsu Higuchi,Tamaki Izume,Sae Okazaki,Masanori Hashimoto,Ritsu Mizutori,Sahoko Tomida,Yumeka Yamauchi,Rei Abe-Yoshizumi,Kota Katayama,Satoshi P. Tsunoda,Satoshi P. Tsunoda,Mikihiro Shibata,Yuji Furutani,Yuji Furutani,Yuji Furutani,Alina Pushkarev,Oded Béjà,Takayuki Uchihashi,Takayuki Uchihashi,Hideki Kandori,Osamu Nureki +27 more
TL;DR: The 2.4-Å-resolution structure of HeR from an uncultured Thermoplasmatales archaeon SG8-52-1 shows that it adopts a similar fold to that of type I rhodopsin—despite the low sequence identity—but there are also several marked differences that provide insights into heliorhodopin function.
82
Schizorhodopsins: A family of rhodopsins from Asgard archaea that function as light-driven inward H+ pumps.
Keiichi Inoue,Satoshi P. Tsunoda,Satoshi P. Tsunoda,Manish Singh,Sahoko Tomida,Shoko Hososhima,Masae Konno,Ryoko Nakamura,Hiroki Watanabe,Paul-Adrian Bulzu,Horia L. Banciu,Adrian-Ştefan Andrei,Takayuki Uchihashi,Rohit Ghai,Oded Béjà,Hideki Kandori +15 more
TL;DR: The function, trimeric structure, and H+ transport mechanism of SzR are similar to that of xenorhodopsin (XeR), a light-driven inward H+ pumping microbial rhodopsins, implying that they evolved convergently.
75
Red-shifting mutation of light-driven sodium-pump rhodopsin
Keiichi Inoue,María del Carmen Marín,María del Carmen Marín,Sahoko Tomida,Ryoko Nakamura,Yuta Nakajima,Massimo Olivucci,Hideki Kandori +7 more
TL;DR: A 40-nm red-shift in the absorption wavelength of a sodium-pump rhodopsin (KR2) is achieved by altering dipole moment of residues around the retinal chromophore without impairing its ion-transport activity.
Long-distance perturbation on Schiff base-counterion interactions by His30 and the extracellular Na+-binding site in Krokinobacter rhodopsin 2.
Arisu Shigeta,Shota Ito,Rina Kaneko,Sahoko Tomida,Keiichi Inoue,Keiichi Inoue,Hideki Kandori,Hideki Kandori,Izuru Kawamura +8 more
TL;DR: Long-distance perturbation of the binding site and Schiff base revealed that a non-transported ion binding at the extracellular site is essential for pumping, and revealed why H30A lacks the proton pumping function.
16
Infrared spectroscopic analysis on structural changes around the protonated Schiff base upon retinal isomerization in light-driven sodium pump KR2.
TL;DR: Comprehensive low-temperature light-induced difference FTIR spectroscopy on isotopically labeled KR2 WT and site-directed mutant proteins found that presence of a positive charge at the position of R109 is prerequisite for the pumping function of KR2.
16