7MC0

Inward facing conformation of the MetNI methionine ABC transporter

7MC0 の概要

• エントリーDOI: 10.2210/pdb7mc0/pdb
• EMDBエントリー: 23752
• 分子名称: ABC transporter, permease protein, ABC transporter, ATP-binding protein (2 entities in total)
• 機能のキーワード: membrane protein
• 由来する生物種: Neisseria meningitidis serogroup B (strain MC58); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 108458.43

構造登録者

Sharaf, N.G.,Rees, D.C. (登録日: 2021-04-01, 公開日: 2021-09-01, 最終更新日: 2025-05-14)

主引用文献

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

実験手法

ELECTRON MICROSCOPY (3.3 Å)