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TitleStructure and function of EfpA as a lipid transporter and its inhibition by BRD-8000.3.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 121, Issue 44, Page e2412653121, Year 2024
Publish dateOct 29, 2024
AuthorsDelin Li / Xiaokang Zhang / Yuanhang Yao / Xue Sun / Junqing Sun / Xiaomin Ma / Kai Yuan / Guijie Bai / Xuefei Pang / Rongmao Hua / Tianling Guo / Yuqian Mi / Lingzhi Wu / Jie Zhang / Yan Wu / Yingxia Liu / Peiyi Wang / Catherine C L Wong / Xiao-Wei Chen / Haixia Xiao / George Fu Gao / Feng Gao /
PubMed AbstractEfpA, the first major facilitator superfamily (MFS) protein identified in (Mtb), is an essential efflux pump implicated in resistance to multiple drugs. EfpA-inhibitors have been developed to kill ...EfpA, the first major facilitator superfamily (MFS) protein identified in (Mtb), is an essential efflux pump implicated in resistance to multiple drugs. EfpA-inhibitors have been developed to kill drug-tolerant Mtb. However, the biological function of EfpA has not yet been elucidated. Here, we present the cryo-EM structures of EfpA complexed with lipids or the inhibitor BRD-8000.3 at resolutions of 2.9 Å and 3.4 Å, respectively. Unexpectedly, EfpA forms an antiparallel dimer. Functional studies reveal that EfpA is a lipid transporter and BRD-8000.3 inhibits its lipid transport activity. Intriguingly, the mutation V319F, known to confer resistance to BRD-8000.3, alters the expression level and oligomeric state of EfpA. Based on our results and the observation of other antiparallel dimers in the MFS family, we propose an antiparallel-function model of EfpA. Collectively, our work provides structural and functional insights into EfpA's role in lipid transport and drug resistance, which would accelerate the development of antibiotics against this promising drug target.
External linksProc Natl Acad Sci U S A / PubMed:39441632 / PubMed Central
MethodsEM (single particle)
Resolution3.41 Å
Structure data

39432

8ynz

EMDB-39432, PDB-8ynz:
The structure of EfpA_BRD-8000.3 complex
Method: EM (single particle) / Resolution: 3.41 Å

Chemicals

PDB-1aqr:
CU-METALLOTHIONEIN FROM SACCHAROMYCES CEREVISIAE, NMR, MINIMIZED AVERAGE STRUCTURE

Source
  • Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (bacteria)
  • mycobacterium tuberculosis h37rv (bacteria)
KeywordsPROTEIN BINDING

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