9VTMSummary for 9VTM
| Entry DOI | 10.2210/pdb9vtm/pdb |
| EMDB information | 65335 |
| Descriptor | Pleiotropic ABC efflux transporter of multiple drugs CDR1, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER (2 entities in total) |
| Functional Keywords | candida albicans, multidrug resistance, substrate efflux cycle, inhibitor, transport protein |
| Biological source | Candida albicans SC5314 |
| Total number of polymer chains | 1 |
| Total formula weight | 170665.85 |
| Authors | |
| Primary citation | Wang, Z.,Yang, S.,Zhang, B.,Jiang, H.,Li, Y.,Gao, R.,Wang, Y.,Fan, F.,Dong, L.,Qiu, J.,Li, X.,Zhou, Y.,Murchie, A.I.H.,Yu, X. Cryo-EM structures of Cdr1 reveal snapshots of substrate transport and diverse inhibitor recognition. Sci Adv, 12:eaef7706-eaef7706, 2026 Cited by PubMed Abstract: In -a World Health Organization fungal priority pathogen-overexpression of the adenosine triphosphate (ATP)-binding cassette transporter Cdr1 drives multidrug resistance. We present seven cryo-electron microscopy structures capturing substrate entry and expulsion. An inward-facing transmembrane channel with three on-off substrate binding sites defines a proposed entry pathway for a single substrate molecule. Coordinated ATP binding to both nucleotide-binding domains induces transmembrane domain closure, driving the substrate expulsion; adenosine diphosphate release following ATP hydrolysis resets the transporter to an inward-open conformation, enabling substrate entry for the next translocation cycle. Structures with three structurally diverse inhibitors resolve two distinct binding modes: one occupying all three substrate sites and another specifically binding two extracellular-proximal sites. These findings provide snapshots of the substrate translocation cycle and structural blueprints for antifungal drug design. PubMed: 42664345DOI: 10.1126/sciadv.aef7706 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.92 Å) |
Structure validation
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