7MBZ

Outward facing conformation of the MetNI methionine ABC transporter in complex with lipo-MetQ

Summary for 7MBZ

• Entry DOI: 10.2210/pdb7mbz/pdb
• EMDB information: 23751
• Descriptor: ABC transporter, permease protein, Lipoprotein, ABC transporter, ATP-binding protein (3 entities in total)
• Functional Keywords: membrane protein
• Biological source: Neisseria meningitidis serogroup B (strain MC58); More
• Total number of polymer chains: 5
• Total formula weight: 141468.68

Authors

Sharaf, N.G.,Rees, D.C. (deposition date: 2021-04-01, release date: 2021-09-01, Last modification date: 2024-05-29)

Primary citation

Sharaf, N.G.,Shahgholi, M.,Kim, E.,Lai, J.Y.,VanderVelde, D.G.,Lee, A.T.,Rees, D.C.
Characterization of the ABC methionine transporter from Neisseria meningitidis reveals that lipidated MetQ is required for interaction.
Elife, 10:-, 2021

PubMed Abstract: 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.

PubMed: 34409939
DOI: 10.7554/eLife.69742

Experimental method

ELECTRON MICROSCOPY (6.4 Å)