Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structure and druggable conformation of the homodimeric lipoprotein transporter of Acinetobacter baumannii.
Journal, issue, pages	Nat Commun, Year 2026
Publish date	Jul 29, 2025
Authors	Song Zhang / Zhuyun Tang / Weiwei Shi / Jiaqi Su / Chao Che / Qi Xing / Maofu Liao / Yanyan Li /
PubMed Abstract	The growing crisis of antimicrobial resistance demands urgent need for antibiotics with alternative targets and modes of action (MOAs). Lipoproteins play crucial roles in bacterial survival and ...The growing crisis of antimicrobial resistance demands urgent need for antibiotics with alternative targets and modes of action (MOAs). Lipoproteins play crucial roles in bacterial survival and immunoregulation. The lipoprotein transporter, known as LolCDE or LolDF, has recently emerged as an effective target for selectively killing pathogenic bacteria such as Acinetobacter baumannii while sparing gut microbiota. While the heterodimeric LolCDE in Escherichia coli has been extensively studied, the druggable pocket and structural dynamics of the distinct homodimeric LolDF that exists in many critical pathogens are poorly understood. Such a knowledge gap limits our ability to exploit the Lol system to develop drugs with desired spectra of antibacterial activity. Here we determine the cryo-EM structures of homodimeric LolDF of A. baumannii in nucleotide-free apo-closed, vanadate-trapped fully closed, and inhibitor-bound open conformations, revealing the distinct structural features and conformational cycle of LolDF. Further cryo-EM, biochemical and functional analyses uncover the MOA of abaucin, a recently identified LolDF-targeting compound, demonstrating how multiple abaucin molecules open LolDF in a stepwise manner to establish an induced-fit pocket. Together, our results advance the understanding of LolDF function and inhibition, and provide the cryptic druggable conformation and specific inhibitor-bound pocket for structure-based drug discovery to target the dynamic lipoprotein transporter in A. baumannii.
External links	Nat Commun / PubMed:42091888
Methods	EM (single particle)
Resolution	3.5 - 4.0 Å
Structure data	65582 EMDB Unreleased entry 9w2w EMDB-65582, PDB-9w2w: Cryo-EM structure of two abaucin-bound LolDF in Acinetobacter baumannii Method: EM (single particle) / Resolution: 3.5 Å 65591 EMDB Unreleased entry 9w35 EMDB-65591, PDB-9w35: Cryo-EM structure of four abaucin-bound LolDF in Acinetobacter baumannii Method: EM (single particle) / Resolution: 3.5 Å 65592 EMDB Unreleased entry 9w36 EMDB-65592, PDB-9w36: Cryo-EM structure of nucleotide-free LolDF in Acinetobacter baumannii Method: EM (single particle) / Resolution: 4.0 Å
Chemicals	ChemComp-R6Q: 1'-[2-[4-(trifluoromethyl)phenyl]ethyl]spiro[1~{H}-3,1-benzoxazine-4,4'-piperidine]-2-one
Source	acinetobacter baumannii (bacteria)
Keywords	MEMBRANE PROTEIN / Acinetobacter baumannii / LolFD / Nanodisc / Inhibitor / nucleotide-free