Cryo-EM structures of E. coli cytochrome bo3 in MSP Nanodiscs
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ABSTRACT:
SUBMITTER: Oliver Biggs Clarke
PROVIDER: EMPIAR-10737 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Cryo-EM structures of <i>Escherichia coli</i> cytochrome <i>bo</i><sub><i>3</i></sub> reveal bound phospholipids and ubiquinone-8 in a dynamic substrate binding site.
Li Jiao J Han Long L Vallese Francesca F Ding Ziqiao Z Choi Sylvia K SK Hong Sangjin S Luo Yanmei Y Liu Bin B Chan Chun Kit CK Tajkhorshid Emad E Zhu Jiapeng J Clarke Oliver O Zhang Kai K Gennis Robert R
Proceedings of the National Academy of Sciences of the United States of America 20210801 34
Two independent structures of the proton-pumping, respiratory cytochrome <i>bo</i><sub><i>3</i></sub> ubiquinol oxidase (cyt <i>bo</i><sub><i>3</i></sub> ) have been determined by cryogenic electron microscopy (cryo-EM) in styrene-maleic acid (SMA) copolymer nanodiscs and in membrane scaffold protein (MSP) nanodiscs to 2.55- and 2.19-Å resolution, respectively. The structures include the metal redox centers (heme <i>b</i>, heme <i>o</i><sub><i>3</i></sub> , and Cu<sub>B</sub>), the redox-active ...[more]
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