2.4.1.292: GalNAc-alpha-(1->4)-GalNAc-alpha-(1->3)-diNAcBac-PP-undecaprenol alpha-1,4-N-acetyl-D-galactosaminyltransferase

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For detailed information about GalNAc-alpha-(1->4)-GalNAc-alpha-(1->3)-diNAcBac-PP-undecaprenol alpha-1,4-N-acetyl-D-galactosaminyltransferase, go to the full flat file.

Reaction

3 UDP-N-acetyl-alpha-D-galactosamine +

Synonyms

PglH, pglH2

ECTree

     2 Transferases

         2.4 Glycosyltransferases

             2.4.1 Hexosyltransferases

                2.4.1.292 GalNAc-alpha-(1->4)-GalNAc-alpha-(1->3)-diNAcBac-PP-undecaprenol alpha-1,4-N-acetyl-D-galactosaminyltransferase

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Results	in table
402	AA Sequence
5	Cloned(Commentary)
2	Crystallization (Commentary)
23	General Information
2	Inhibitors
2	Localization
1	Molecular Weight [Da]
7	Natural Substrates/ Products (Substrates)
49	Organism
1	Pathway
3	pH Optimum
32	Protein Variants
3	Purification (Commentary)
2	Reaction
12	Reference
13	Substrates and Products (Substrate)
3	Subunits
10	Synonyms
1	Systematic Name
1	Temperature Optimum [°C]
1	Temperature Stability [°C]
11	Turnover Number [1/s]

Crystallization

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Crystallization on EC 2.4.1.292 - GalNAc-alpha-(1->4)-GalNAc-alpha-(1->3)-diNAcBac-PP-undecaprenol alpha-1,4-N-acetyl-D-galactosaminyltransferase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

crystal structures of PglH in a binary complex with UDP-GalNAc and two ternary complexes containing a chemo-enzymatically generated lipid-linked oligosaccharide analogue and either UDP or synthetic, nonhydrolyzable UDP-CH2-GalNAc. PglH contains an amphipathic helix that has a dual role of facilitating membrane attachment and glycan counting. The helix contains three positively charged side chains that can bind the diphosphate group of the lipid-linked oligosaccharide substrate and thus limit the addition of GalNAc units to three

Campylobacter jejuni

O86151

759837

purified recombinant His-tagged PglH (native or the selenomethionine derivative) in three distinct states, including a binary complex with UDP-GalNAc and two ternary complexes containing a chemo-enzymatically generated LLO analogue and either UDP or synthetic, nonhydrolyzable UDP-CH2-GalNAc, apoenzyme by vapor diffusion in sitting or hanging drops at 20°C, using a reservoir containing 0.2M KI, 0.1M MOPS, pH 7.2, and 17% PEG 3350, the volume ratio of protein to reservoir is 1:1, for PglH with bound acceptor substrate, concentrated PglH is incubated with synthetic LLO at 0.6 mM and UDP or UDP-CH2-GalNAc at 2 mM (final concentrations) for 15 min, crystallization is performed by vapor diffusion in sitting drops or hanging drops at 20°C using a reservoir containing 0.2 M Ammonium acetate, 0.1 M ADA 6.3, and 21-22% PEG 3350, the volume ratio of protein to reservoir is 1:1, 1-4 days, X-ray diffraction structure determination and analysis at 2.3-3.3 A resolution

Campylobacter jejuni

O86151

759837