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Conformational dynamics in binding-protein-independent mutant of the Escherichia coli maltose transporter, MalG511 and its interaction with maltose binding protein

MalG511 is a genetically selected binding-protein-independent mutant of Escherichia coli maltose transporter (MalFGK(2)), which retains specificity for maltose and shows a high basal ATPase activity in the absence of maltose binding protein (MBP). It shows an intriguing biphasic behavior in maltose...

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Publicado en:Biochemistry
Autores principales: Bajaj, Ruchika, Park, Mariana I., Stauffacher, Cynthia V., Davidson, Amy L.
Formato: Artigo
Lenguaje:Inglês
Publicado: 2018
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Acceso en línea:https://ncbi.nlm.nih.gov/pmc/articles/PMC5964036/
https://ncbi.nlm.nih.gov/pubmed/29637782
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/acs.biochem.8b00266
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