Article
Structural basis for unique color tuning mechanism in heliorhodopsin.
Biochemical and biophysical research communications - 10 Dec 2020
Tanaka Tatsuki, Singh Manish, Shihoya Wataru, Yamashita Keitaro, Kandori Hideki, Nureki Osamu
Abstract excerpt
Microbial rhodopsins comprise an opsin protein with seven transmembrane helices and a retinal as the chromophore. An all-trans retinal is covalently bonded to a lysine residue through the retinal Schiff base (RSB) and stabilized by a negatively charged counterion. The distance between the RSB and counterion is closely related to the light energy absorption. However, in heliorhodopsin-48C12 (HeR-48C12), while E107...
Topics
- Amino Acid Substitution
- Archaeal Proteins
- Binding Sites
- Cloning, Molecular
- Color
- Crystallography, X-Ray
- Escherichia coli
- Gene Expression
- Genetic Vectors
- Models, Molecular
- Mutation
- Protein Binding
- Protein Conformation, alpha-Helical
- Protein Conformation, beta-Strand