Crystal structure of CmABCB1 multi-drug exporter in lipidic mesophase revealed by LCP-SFX.

ABSTRACT: CmABCB1 is a Cyanidioschyzon merolae homolog of human ABCB1, a well known ATP-binding cassette (ABC) transporter responsible for multi-drug resistance in various cancers. Three-dimensional structures of ABCB1 homologs have revealed the snapshots of inward- and outward-facing states of the transporters in action. However, sufficient information to establish the sequential movements of the open-close cycles of the alternating-access model is still lacking. Serial femtosecond crystallography (SFX) using X-ray free-electron lasers has proven its worth in determining novel structures and recording sequential conformational changes of proteins at room temperature, especially for medically important membrane proteins, but it has never been applied to ABC transporters. In this study, 7.7 mo

SUBMITTER: Pan D 

PROVIDER: S-EPMC8733880 | biostudies-literature | 2022 Jan

REPOSITORIES: biostudies-literature