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.

Journal of Bacteriology- United States

doi 10.1128/jb.177.18.5364-5367.1995

Full Text

Abstract

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Date

January 1, 1995

Authors

E Schneider

S Hunke

S Tebbe

Publisher

American Society for Microbiology

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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.

Journal of Bacteriology- United States

Full Text

Abstract

Categories

Date

Authors

Publisher

Related search

Topography of the Surface of the Signal-Transducing Protein EIIAGlcThat Interacts With the MalK Subunits of the Maltose ATP-binding Cassette Transporter (MalFGK2) ofSalmonella Typhimurium

Binding Specificity of the Periplasmic Oligopeptide-Binding Protein From Escherichia Coli.

Conformational Dynamics in the Binding-Protein-Independent Mutant of the Escherichia Coli Maltose Transporter MalG511, and Its Interaction With Maltose Binding Protein

Both Maltose-Binding Protein and ATP Are Required for Nucleotide-Binding Domain Closure in the Intact Maltose ABC Transporter

Expression of Membrane Proteins From Mycobacterium Tuberculosis in Escherichia Coli as Fusions With Maltose Binding Protein

Vacuolar Import of Phosphatidylcholine Requires the ATP-Binding Cassette Transporter Ybt1

Structure and Metal Binding Properties of ZnuA, a Periplasmic Zinc Transporter From Escherichia Coli

Escherichia Coli Signal Peptides Direct Inefficient Secretion of an Outer Membrane Protein (OmpA) and Periplasmic Proteins (Maltose-Binding Protein, Ribose-Binding Protein, and Alkaline Phosphatase) in Bacillus Subtilis.

The ATP Binding Cassette Transporter GeneCgCDR1 From Candida Glabrata Is Involved in the Resistance of Clinical Isolates to Azole Antifungal Agents