Characterization of the structural requirements for assembly and nucleotide binding of an ATP-binding cassette transporter. The maltose transport system of Escherichia coli

The periplasmic maltose-binding protein-dependent, maltose transport system of Escherichia coli is a well studied member of the ATP-binding cassette family of transport ATPases. In addition to the water-soluble maltose-binding protein, the system comprises three membrane proteins, MalF, MalG, and Ma...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	The Journal of biological chemistry 1993-11, Vol.268 (31), p.23685-23696
Hauptverfasser:	PANAGIOTIDIS, C. H, REYES, M, SIEVERTSEN, A, BOOS, W, SHUMAN, H. A
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphate - metabolism Analytical, structural and metabolic biochemistry ATP-Binding Cassette Transporters Bacterial Proteins - metabolism Base Sequence Binding and carrier proteins Binding Sites Biological and medical sciences Biological Transport, Active Carrier Proteins - metabolism Cell Compartmentation Cell Membrane - metabolism Cross-Linking Reagents DNA Mutational Analysis DNA Primers Escherichia coli - chemistry Escherichia coli - metabolism Escherichia coli Proteins Fundamental and applied biological sciences. Psychology In Vitro Techniques Macromolecular Substances Maltose - metabolism Maltose-Binding Proteins Membrane Proteins - metabolism Molecular Sequence Data Monosaccharide Transport Proteins Periplasmic Binding Proteins Proteins Recombinant Proteins Structure-Activity Relationship
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Schreiben Sie den ersten Kommentar!