期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 59, 期 9, 页码 3523-3528出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201914411
关键词
lipid binding; membrane protein structure; molecular dynamics; native mass spectrometry
资金
- Ingvar Carlsson Award from Swedish Foundation for Strategic Research
- VR starting grant
- KI-StratNeuro starting grant
- VR grant [2013_08807]
- Wellcome Trust [104633/Z/14/Z]
- ERC Advanced Grant ENABLE [641317]
- MRC Programme Grant [MR/N020413/1]
- Wellcome [208361/Z/17/Z]
- MRC [MR/S009213/1]
- BBSRC [BB/P01948X/1, BB/R002517/1 BB/S003339/1]
- EPSRC [EP/P020232/1, EP/R029407/1]
- KI faculty
- BBSRC [BB/S003339/1, BB/P01948X/1, BB/R002517/1] Funding Source: UKRI
- EPSRC [EP/R029407/1] Funding Source: UKRI
- MRC [MR/N020413/1] Funding Source: UKRI
- European Research Council (ERC) [641317] Funding Source: European Research Council (ERC)
Membrane proteins engage in a variety of contacts with their surrounding lipids, but distinguishing between specifically bound lipids, and non-specific, annular interactions is a challenging problem. Applying native mass spectrometry to three membrane protein complexes with different lipid-binding properties, we explore the ability of detergents to compete with lipids bound in different environments. We show that lipids in annular positions on the presenilin homologue protease are subject to constant exchange with detergent. By contrast, detergent-resistant lipids bound at the dimer interface in the leucine transporter show decreased k(off) rates in molecular dynamics simulations. Turning to the lipid flippase MurJ, we find that addition of the natural substrate lipid-II results in the formation of a 1:1 protein-lipid complex, where the lipid cannot be displaced by detergent from the highly protected active site. In summary, we distinguish annular from non-annular lipids based on their exchange rates in solution.
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