4.5 Article

ATP binding drives substrate capture in an ECF transporter by a release-and-catch mechanism

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NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 22, 期 7, 页码 565-+

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NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.3040

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  1. American Heart Association
  2. US National Institutes of Health (NIH) [F32-HL091618]
  3. NIH [R01DK099023, R01-DK073973, R01-GM093825, R01-MH083840]

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ECF transporters are a family of active transporters for vitamins. They are composed of four subunits: a membrane-embedded substrate-binding subunit (EcfS), a transmembrane coupling subunit (EcfT) and two ATP-binding-cassette ATPases (EcfA and EcfA'). We have investigated the mechanism of the ECF transporter for riboflavin from the pathogen Listeria monocytogenes, LmECF-RibU. Using structural and biochemical approaches, we found that ATP binding to the EcfAA' ATPases drives a conformational change that dissociates the S subunit from the EcfAA'T ECF module. Upon release from the ECF module, the RibU S subunit then binds the riboflavin transport substrate. We also find that S subunits for distinct substrates compete for the ATP-bound state of the ECF module. Our results explain how ECF transporters capture the transport substrate and reproduce the in vivo observations on S-subunit competition for which the family was named.

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