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-Structure paper
タイトル | Characterization of the ABC methionine transporter from reveals that lipidated MetQ is required for interaction. |
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ジャーナル・号・ページ | Elife, Vol. 10, Year 2021 |
掲載日 | 2021年8月19日 |
著者 | Naima G Sharaf / Mona Shahgholi / Esther Kim / Jeffrey Y Lai / David G VanderVelde / Allen T Lee / Douglas C Rees / |
PubMed 要旨 | 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 ...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. |
リンク | Elife / PubMed:34409939 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.3 - 6.4 Å |
構造データ | EMDB-23751, PDB-7mbz: EMDB-23752, PDB-7mc0: |
由来 |
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キーワード | MEMBRANE PROTEIN |