Characterization of the ABC methionine transporter from Neisseria meningitidis reveals that lipidated MetQ is required for interaction
NmMetQ is a substrate-binding protein (SBP) from Neisseria meningitidis 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 sp...
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eLife Sciences Publications Ltd
2021-08-01
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Series: | eLife |
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Online Access: | https://elifesciences.org/articles/69742 |
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author | Naima G Sharaf Mona Shahgholi Esther Kim Jeffrey Y Lai David G VanderVelde Allen T Lee Douglas C Rees |
author_facet | Naima G Sharaf Mona Shahgholi Esther Kim Jeffrey Y Lai David G VanderVelde Allen T Lee Douglas C Rees |
author_sort | Naima G Sharaf |
collection | DOAJ |
description | NmMetQ is a substrate-binding protein (SBP) from Neisseria meningitidis 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. |
first_indexed | 2024-04-12T09:52:05Z |
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institution | Directory Open Access Journal |
issn | 2050-084X |
language | English |
last_indexed | 2024-04-12T09:52:05Z |
publishDate | 2021-08-01 |
publisher | eLife Sciences Publications Ltd |
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spelling | doaj.art-644cf02d64a6410194394509bed6ace72022-12-22T03:37:48ZengeLife Sciences Publications LtdeLife2050-084X2021-08-011010.7554/eLife.69742Characterization of the ABC methionine transporter from Neisseria meningitidis reveals that lipidated MetQ is required for interactionNaima G Sharaf0https://orcid.org/0000-0002-3662-9228Mona Shahgholi1Esther Kim2Jeffrey Y Lai3David G VanderVelde4https://orcid.org/0000-0002-2907-0366Allen T Lee5Douglas C Rees6https://orcid.org/0000-0003-4073-1185Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, United States; Howard Hughes Medical Institute, California Institute of Technology, Pasadena, United StatesDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, United StatesDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, United StatesDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, United States; Howard Hughes Medical Institute, California Institute of Technology, Pasadena, United StatesDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, United StatesDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, United States; Howard Hughes Medical Institute, California Institute of Technology, Pasadena, United StatesDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, United States; Howard Hughes Medical Institute, California Institute of Technology, Pasadena, United StatesNmMetQ is a substrate-binding protein (SBP) from Neisseria meningitidis 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.https://elifesciences.org/articles/69742lipoproteinABC transportersNeisseria meningitidismethionine importerssingle particle cryoemfluorine solution nmr |
spellingShingle | Naima G Sharaf Mona Shahgholi Esther Kim Jeffrey Y Lai David G VanderVelde Allen T Lee Douglas C Rees Characterization of the ABC methionine transporter from Neisseria meningitidis reveals that lipidated MetQ is required for interaction eLife lipoprotein ABC transporters Neisseria meningitidis methionine importers single particle cryoem fluorine solution nmr |
title | Characterization of the ABC methionine transporter from Neisseria meningitidis reveals that lipidated MetQ is required for interaction |
title_full | Characterization of the ABC methionine transporter from Neisseria meningitidis reveals that lipidated MetQ is required for interaction |
title_fullStr | Characterization of the ABC methionine transporter from Neisseria meningitidis reveals that lipidated MetQ is required for interaction |
title_full_unstemmed | Characterization of the ABC methionine transporter from Neisseria meningitidis reveals that lipidated MetQ is required for interaction |
title_short | Characterization of the ABC methionine transporter from Neisseria meningitidis reveals that lipidated MetQ is required for interaction |
title_sort | characterization of the abc methionine transporter from neisseria meningitidis reveals that lipidated metq is required for interaction |
topic | lipoprotein ABC transporters Neisseria meningitidis methionine importers single particle cryoem fluorine solution nmr |
url | https://elifesciences.org/articles/69742 |
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