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Literature summary for 2.7.1.181 extracted from

  • Hagelueken, G.; Huang, H.; Clarke, B.R.; Lebl, T.; Whitfield, C.; Naismith, J.H.
    Structure of WbdD: a bifunctional kinase and methyltransferase that regulates the chain length of the O antigen in Escherichia coli O9a (2012), Mol. Microbiol., 86, 730-742.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
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Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
2.2 A resolution structure reveals a bacterial methyltransferase domain joined to a eukaryotic kinase domain. The kinase domain is again fused to an extended C-terminal coiled-coil domain reminiscent of eukaryotic Myotonic Dystrophy Protein Kinase family kinases. Structures of co-complexes with two known eukaryotic protein kinase inhibitors which are potent inhibitors in vitro, but do not show any in vivo activity Escherichia coli

Protein Variants

Protein Variants Comment Organism
D350A 88.8% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 95.2% with substrate D-mannose Escherichia coli
D351A 0.9% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 1.1% with substrate D-mannose Escherichia coli
D351E 4.5% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 1.5% with substrate D-mannose Escherichia coli
DELTA398-418 6.7% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 4.7% with substrate D-mannose Escherichia coli
E274A 45.4% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 66.6% with substrate D-mannose Escherichia coli
H132A complete loss of activity Escherichia coli
H133A complete loss of activity Escherichia coli
N34D/Q35E/H197E complete loss of activity Escherichia coli
R203A complete loss of activity Escherichia coli
R270A 72.8% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 85.7% with substrate D-mannose Escherichia coli
W355F 72.4% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 1.9% with substrate D-mannose Escherichia coli
W355H 48.7% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 50.7% with substrate D-mannose Escherichia coli
Y16F complete loss of activity Escherichia coli
Y230F 0.1% of wild-type activity with substrate 2-alpha-D-mannosyl-D-mannose, 2.5% with substrate D-mannose Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli J7I4B7
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-
Escherichia coli O9a J7I4B7
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 2-alpha-D-mannosyl-D-mannose
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Escherichia coli ADP + 3-O-phospho-2-alpha-D-mannosyl-D-mannose
-
?
ATP + 2-alpha-D-mannosyl-D-mannose
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Escherichia coli O9a ADP + 3-O-phospho-2-alpha-D-mannosyl-D-mannose
-
?
ATP + D-mannose
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Escherichia coli ADP + 3-O-phospho-D-mannose
-
?
ATP + D-mannose
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Escherichia coli O9a ADP + 3-O-phospho-D-mannose
-
?