9kwi | pdb_00009kwi

Cryo-EM structure of MsRv1273c/72c(E553Q) mutant from Mycobacterium smegmatis in the ATP-bound Occ state

spinqualitylabelsall models 9kwi, resolution 3.19Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9kwi is a 2 chain structure with sequence from Mycolicibacterium smegmatis MC2 155. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.19Å Ligands: ATP, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0R271_MYCS2 Publication Abstract from PubMed Heterodimeric ATP-binding cassette (ABC) transporters containing one catalytically impaired degenerate nucleotide-binding site (NBS) have a mechanism different from those with two active NBSs. However, the structural basis of their transport mechanism remains to be explained. Here, we determine mycobacterial MsRv1273c/72c to be an isoniazid efflux pump and determine several structures by cryo-electron microscopy showing specific asymmetrical features including an N-terminal extending loop and a periplasmic helical hairpin only found in MsRv1272c. In addition, we capture three distinct asymmetric states where the nucleotide-binding domains are partially dimerized at the degenerate site. Using these intermediate states, the D-WalkerB loop and X-signature loop of MsRv1272c modulate and couple the function of both NBSs through conformational changes. Thus, these data provide insights into the mechanism of this heterodimeric ABC transporter containing a degenerate NBS. The structures also provide a framework for the rational design of anti-tuberculosis drugs targeting this drug-efflux pump. Structure and mechanism of a mycobacterial isoniazid efflux pump MsRv1273c/72c with a degenerate nucleotide-binding site.,Yu J, Lan Y, Zhu C, Chen Z, Pan J, Shi Y, Yang L, Hu T, Gao Y, Zhao Y, Chen X, Yang X, Lu S, Guddat LW, Yang H, Rao Z, Li J Nat Commun. 2025 Apr 28;16(1):3969. doi: 10.1038/s41467-025-59300-5. PMID:40295516 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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