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Characterization of the ABC Methionine Transporter from Reveals That Lipidated MetQ is Required for Interaction

Overview
Journal Elife
Specialty Biology
Date 2021 Aug 19
PMID 34409939
Citations 5
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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.

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References
1.
Parra M, Shaffer S, Hajjar A, Gallis B, Hager A, Goodlett D . Identification, cloning, expression, and purification of Francisella lpp3: an immunogenic lipoprotein. Microbiol Res. 2009; 165(7):531-45. DOI: 10.1016/j.micres.2009.11.004. View

2.
Oldham M, Chen S, Chen J . Structural basis for substrate specificity in the Escherichia coli maltose transport system. Proc Natl Acad Sci U S A. 2013; 110(45):18132-7. PMC: 3831462. DOI: 10.1073/pnas.1311407110. View

3.
Krismer B, Liebeke M, Janek D, Nega M, Rautenberg M, Hornig G . Nutrient limitation governs Staphylococcus aureus metabolism and niche adaptation in the human nose. PLoS Pathog. 2014; 10(1):e1003862. PMC: 3894218. DOI: 10.1371/journal.ppat.1003862. View

4.
Mastronarde D . Automated electron microscope tomography using robust prediction of specimen movements. J Struct Biol. 2005; 152(1):36-51. DOI: 10.1016/j.jsb.2005.07.007. View

5.
Castaneda-Roldan E, Ouahrani-Bettache S, Saldana Z, Avelino F, Rendon M, Dornand J . Characterization of SP41, a surface protein of Brucella associated with adherence and invasion of host epithelial cells. Cell Microbiol. 2006; 8(12):1877-87. DOI: 10.1111/j.1462-5822.2006.00754.x. View