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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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| Main Authors: | , , , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado: |
2009
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| Assuntos: | |
| Acceso en liña: | 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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