The Topology of the l-Arginine Exporter ArgO Conforms to an Nin-Cout Configuration in Escherichia coli: Requirement for the Cytoplasmic N-Terminal Domain, Functional Helical Interactions, and an Aspartate Pair for ArgO Function.
Pathania, Amit
The Topology of the l-Arginine Exporter ArgO Conforms to an Nin-Cout Configuration in Escherichia coli: Requirement for the Cytoplasmic N-Terminal Domain, Functional Helical Interactions, and an Aspartate Pair for ArgO Function. [electronic resource] - Journal of bacteriology 12 2016 - 3186-3199 p. digital
Publication Type: Journal Article
1098-5530
10.1128/JB.00423-16 doi
Amino Acid Motifs
Arginine--metabolism
Aspartic Acid--metabolism
Biological Transport
Escherichia coli--chemistry
Escherichia coli Proteins--chemistry
Gene Expression Regulation, Bacterial
Protein Conformation
Protein Domains
The Topology of the l-Arginine Exporter ArgO Conforms to an Nin-Cout Configuration in Escherichia coli: Requirement for the Cytoplasmic N-Terminal Domain, Functional Helical Interactions, and an Aspartate Pair for ArgO Function. [electronic resource] - Journal of bacteriology 12 2016 - 3186-3199 p. digital
Publication Type: Journal Article
1098-5530
10.1128/JB.00423-16 doi
Amino Acid Motifs
Arginine--metabolism
Aspartic Acid--metabolism
Biological Transport
Escherichia coli--chemistry
Escherichia coli Proteins--chemistry
Gene Expression Regulation, Bacterial
Protein Conformation
Protein Domains