2.4.1.B64: glucosyltransferase Waag

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For detailed information about glucosyltransferase Waag, go to the full flat file.

Reaction

alpha-L-glycero-D-manno-heptosyl-(1->3)-alpha-L-glycero-D-manno-heptosyl-(1->5)-[(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)]-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose

alpha-D-glucosyl-(1->3)-alpha-L-glycero-D-manno-heptosyl-(1->3)-alpha-L-glycero-D-manno-heptosyl-(1->5)-[(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->4)]-(3-deoxy-alpha-D-manno-oct-2-ulopyranosylonate)-(2->6)-2-deoxy-2-[[(3R)-3-(dodecanoyloxy)tetradecanoyl]amino]-3-O-[(3R)-3-(tetradecanoyloxy)tetradecanoyl]-4-O-phospho-beta-D-glucopyranosyl-(1->6)-2-deoxy-3-O-[(3R)-3-hydroxytetradecanoyl]-2-[[(3R)-3-hydroxytetradecanoyl]amino]-1-O-phosphono-alpha-D-glucopyranose

Synonyms

(heptosyl)2-alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid A:UDP-alpha-D-glucose glucosyltransferase, core glucosyltransferase, glycosyltransferase WaaG, lipopolysaccharide core biosynthesis protein, lipopolysaccharide glucosyltransferase I, LPS glucosyltransferase I, RfaG, UDP-glucose:(heptosyl) lipopolysaccharide alpha-1,3-glucosyltransferase, WaaG

ECTree

2 Transferases

2.4 Glycosyltransferases

2.4.1 Hexosyltransferases

2.4.1.B64 glucosyltransferase Waag

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Results	in table
4	Activating Compound
2	AA Sequence
2	Application
4	Cloned(Commentary)
2	Crystallization (Commentary)
7	General Information
1	IC50 Value
4	Inhibitors
2	KM Value [mM]
1	Localization
1	Metals/Ions
2	Natural Substrates/ Products (Substrates)
10	Organism
3	Protein Variants
3	Purification (Commentary)
1	Reaction
10	Reference
5	Substrates and Products (Substrate)
17	Synonyms
1	Systematic Name
2	Turnover Number [1/s]

Crystallization

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Crystallization on EC 2.4.1.B64 - glucosyltransferase Waag

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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

P25740

735778

crystals of the enzyme and of its selenomethionine derivative are grown in 0.1 M MES (pH 6.75), 0.2 M NaBr, and 15% PEG 3350 at a protein concentration of 10 mg/ml. Microseeding is necessary to achieve reproducibility of the crystals. Crystals of the complex of the enzyme with UDP-2F-glucose are prepared by addition of 10 mM UDP-2F-glucose to the protein solution prior to crystallization. The structure of the enzyme is solved by single-wavelength anomalous dispersion with a selenomethionine version of the protein, at a resolution of 1.6 A, in the presence of UDP

Escherichia coli

P25740

727285