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8YR0

Cryo-EM Structure of AdeG from Acinetobacter baumannii

Summary for 8YR0
Entry DOI10.2210/pdb8yr0/pdb
EMDB information39532
DescriptorCation/multidrug efflux pump, DODECYL-BETA-D-MALTOSIDE (2 entities in total)
Functional Keywordsefflux pump, acinetobacter baumannii, multidrug resistance, adeg, membrane protein
Biological sourceAcinetobacter baumannii
Total number of polymer chains3
Total formula weight338944.77
Authors
Ouyang, Z.,Wen, Y.,Zhu, L. (deposition date: 2024-03-20, release date: 2025-01-01, Last modification date: 2026-07-15)
Primary citationOuyang, Z.,He, W.,Wu, D.,An, H.,Duan, L.,Jiao, M.,He, X.,Yu, Q.,Zhang, J.,Qin, Q.,Wang, R.,Zheng, F.,Hwang, P.M.,Hua, X.,Zhu, L.,Wen, Y.
Cryo-EM structure and complementary drug efflux activity of the Acinetobacter baumannii multidrug efflux pump AdeG.
Structure, 33:539-551.e4, 2025
Cited by
PubMed Abstract: Multidrug-resistant Acinetobacter baumannii has emerged as one of the most antibiotic-resistant bacterial pathogens associated with nosocomial infection, with its resistance highly depending on multiple multidrug efflux pumps. Here, we report the cryoelectron microscopy (cryo-EM) structure of Acinetobacter drug efflux G (AdeG), the inner membrane component of one of three important resistance-nodulation-cell division (RND) pump family members in A. baumannii, which is involved in drug resistance to chloramphenicol, trimethoprim, ciprofloxacin, and clindamycin. We systematically compare the structures and substrate binding specificities of AdeG, AdeB, and AdeJ multidrug efflux pumps via molecular docking, revealing potential determinants for drug binding. Knockout experiments demonstrate a functional complementarity between AdeABC, AdeFGH, and AdeIJK. Our study provides a structural understanding of A. baumannii multidrug efflux pump AdeG and reveals complementary drug efflux activity between AdeG and other RND efflux pumps, which may promote further rational drug discovery efforts targeting multidrug efflux pumps.
PubMed: 39798571
DOI: 10.1016/j.str.2024.12.009
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.06 Å)
Structure validation

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