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Nucleotide-free MalK Drives the Transition of the Maltose Transporter to the Inward-facing Conformation
The complex MalFGK(2) hydrolyzes ATP and alternates between inward- and outward-facing conformations during maltose transport. It has been shown that ATP promotes closure of MalK(2) and opening of MalFG toward the periplasm. Yet, why the transporter rests in a conformation facing the cytosol in the...
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| Main Authors: | , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
American Society for Biochemistry and Molecular Biology
2014
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3975029/ https://ncbi.nlm.nih.gov/pubmed/24526688 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M113.545525 |
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