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Alternating access in maltose transporter mediated by rigid-body rotations

ATP-binding cassette transporters couple ATP hydrolysis to substrate translocation through an alternating access mechanism, but the nature of the conformational changes in a transport cycle remains elusive. Previously we reported the structure of the maltose transporter MalFGK(2) in an outward-facin...

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Bibliografski detalji
Glavni autori: Khare, Dheeraj, Oldham, Michael L., Orelle, Cedric, Davidson, Amy L., Chen, Jue
Format: Artigo
Jezik:Inglês
Izdano: 2009
Teme:
Online pristup:https://ncbi.nlm.nih.gov/pmc/articles/PMC2714826/
https://ncbi.nlm.nih.gov/pubmed/19250913
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.molcel.2009.01.035
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