Literature summary for 2.4.1.B64 extracted from

Liebau, J.; Pettersson, P.; Szpryngiel, S.; Maeler, L.
Membrane interaction of the glycosyltransferase WaaG (2015), Biophys. J., 109, 552-563.

Search for more literature for 2.4.1.B64

Crystallization (Commentary)

Crystallization (Comment)	Organism
an exposed and largely alpha-helical 30-residue sequence, with a net positive charge and several aromatic amino acids, is the putative membrane-interacting region of WaaG. In the presence of dodecylphosphocholine, the membrane-interacting region adopts a three-dimensional structure remarkably similar to the segment in the crystal structure. The interaction of WaaG is conferred at least in part by the membrane-interacting region and electrostatic interactions play a key role in binding. During anchoring of WaaG to the inner membrane of Escherichia coli, the central part of membrane-interacting region inserts into one leaflet of the bilayer. In this model, electrostatic interactions as well as surface-exposed Tyr residues bind WaaG to the membrane	Escherichia coli

Crystallization (Comment)

Organism

an exposed and largely alpha-helical 30-residue sequence, with a net positive charge and several aromatic amino acids, is the putative membrane-interacting region of WaaG. In the presence of dodecylphosphocholine, the membrane-interacting region adopts a three-dimensional structure remarkably similar to the segment in the crystal structure. The interaction of WaaG is conferred at least in part by the membrane-interacting region and electrostatic interactions play a key role in binding. During anchoring of WaaG to the inner membrane of Escherichia coli, the central part of membrane-interacting region inserts into one leaflet of the bilayer. In this model, electrostatic interactions as well as surface-exposed Tyr residues bind WaaG to the membrane

Escherichia coli

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P25740	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining

Synonyms

Synonyms	Comment	Organism
RfaG	-	Escherichia coli

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Release 2023.1 (January 2023)