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TitleMolecular Basis for the Activation of MsbA by Divalent Metals.
Journal, issue, pagesJ Am Chem Soc, Vol. 147, Issue 35, Page 31488-31496, Year 2025
Publish dateSep 3, 2025
AuthorsJixing Lyu / Hanieh Bahramimoghaddam / Tianqi Zhang / Elena Scott / Sangho D Yun / Gaya P Yadav / Minglei Zhao / David Russell / Arthur Laganowsky /
PubMed AbstractProteins involved in the biogenesis of lipopolysaccharide (LPS), a lipid exclusive to Gram-negative bacteria, are promising candidates for drug discovery. Specifically, the ABC transporter MsbA plays ...Proteins involved in the biogenesis of lipopolysaccharide (LPS), a lipid exclusive to Gram-negative bacteria, are promising candidates for drug discovery. Specifically, the ABC transporter MsbA plays a crucial role in translocating an LPS precursor from the cytoplasmic to the periplasmic facing leaflet of the inner membrane, and small molecules that inhibit its function exhibit bactericidal activity. Here, we use native mass spectrometry (MS) to determine lipid binding affinities of MsbA from (PaMsbA), a Gram-negative bacteria associated with hospital-acquired infections, in different conformations. Unlike the transporter from , we show that the ATPase activity of PaMsbA is stimulated by Zn, Ni, and Mn and successfully trapping the protein with vanadate requires one of these metal ions. We also present cryogenic-electron microscopy structures of PaMsbA in occluded and open outward-facing conformations determined to resolutions of 2.58 and 2.44 Å, respectively. The structures reveal a triad of histidine residues, and mutation of these residues abolishes Zn binding and stimulation of PaMsbA activity by metal ions. Together, our studies provide insight into the structure of PaMsbA and its lipid binding preferences and reveal that a subset of divalent metals stimulates its ATPase activity.
External linksJ Am Chem Soc / PubMed:40851428 / PubMed Central
MethodsEM (single particle)
Resolution2.44 - 2.58 Å
Structure data

44444

9bd6

EMDB-44444, PDB-9bd6:
PaMsbA in an occluded, outward conformation
Method: EM (single particle) / Resolution: 2.58 Å

44445

9bd7

EMDB-44445, PDB-9bd7:
PaMsbA in an open, outward conformation
Method: EM (single particle) / Resolution: 2.44 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-AD9:
ADP METAVANADATE

ChemComp-LMT:
DODECYL-BETA-D-MALTOSIDE / detergent*YM

Source
  • pseudomonas aeruginosa (bacteria)
KeywordsTRANSLOCASE / MsbA / zinc / membrane protein

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