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TitleCharacterization of the ABC methionine transporter from reveals that lipidated MetQ is required for interaction.
Journal, issue, pagesElife, Vol. 10, Year 2021
Publish dateAug 19, 2021
AuthorsNaima G Sharaf / Mona Shahgholi / Esther Kim / Jeffrey Y Lai / David G VanderVelde / Allen T Lee / Douglas C Rees /
PubMed AbstractNmMetQ is a substrate-binding protein (SBP) from that has been identified as a surface-exposed candidate antigen for meningococcal vaccines. However, this location for NmMetQ challenges the ...NmMetQ is a substrate-binding protein (SBP) from that has been identified as a surface-exposed candidate antigen for meningococcal vaccines. However, this location for NmMetQ challenges the prevailing view that SBPs in Gram-negative bacteria are localized to the periplasmic space to promote interaction with their cognate ABC transporter embedded in the bacterial inner membrane. To elucidate the roles of NmMetQ, we characterized NmMetQ with and without its cognate ABC transporter (NmMetNI). Here, we show that NmMetQ is a lipoprotein (lipo-NmMetQ) that binds multiple methionine analogs and stimulates the ATPase activity of NmMetNI. Using single-particle electron cryo-microscopy, we determined the structures of NmMetNI in the presence and absence of lipo-NmMetQ. Based on our data, we propose that NmMetQ tethers to membranes via a lipid anchor and has dual function and localization, playing a role in NmMetNI-mediated transport at the inner membrane and moonlighting on the bacterial surface.
External linksElife / PubMed:34409939 / PubMed Central
MethodsEM (single particle)
Resolution3.3 - 6.4 Å
Structure data

23751

7mbz

EMDB-23751, PDB-7mbz:
Outward facing conformation of the MetNI methionine ABC transporter in complex with lipo-MetQ
Method: EM (single particle) / Resolution: 6.4 Å

23752

7mc0

EMDB-23752, PDB-7mc0:
Inward facing conformation of the MetNI methionine ABC transporter
Method: EM (single particle) / Resolution: 3.3 Å

Source
  • Neisseria meningitidis serogroup B (bacteria)
  • neisseria meningitidis serogroup b (strain mc58) (bacteria)
KeywordsMEMBRANE PROTEIN

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