Novel Missense Mutations That Affect the Transport Function of MalK, the ATP-Binding-Cassette Subunit of the Salmonella enterica Serovar Typhimurium Maltose Transport System

Míreanna Comhchosúla

• The MalK protein of the ATP-binding cassette transporter for maltose of Escherichia coli is accessible to protease digestion from the periplasmic side of the membrane.
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  Foilsithe: (1995)
• Evidence from Mutational Analysis for a Single Transmembrane Substrate Binding Site in the Histidine ATP-Binding Cassette Transporter of Salmonella enterica Serovar Typhimurium
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  Foilsithe: (2018)
• Domain Structure of the ATP-Binding-Cassette Protein MalK of Salmonella typhimurium as Assessed by Coexpressed Half Molecules and LacK′-′MalK Chimeras
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  Foilsithe: (1998)
• The MalF P2 Loop of the ATP-Binding Cassette Transporter MalFGK(2) from Escherichia coli and Salmonella enterica Serovar Typhimurium Interacts with Maltose Binding Protein (MalE) throughout the Catalytic Cycle
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  Foilsithe: (2009)
• Negative Stain Single-particle EM of the Maltose Transporter in Nanodiscs Reveals Asymmetric Closure of MalK(2) and Catalytic Roles of ATP, MalE, and Maltose
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  Foilsithe: (2017)