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Literature summary for 2.1.1.17 extracted from

  • Danne, L.; Aktas, M.; Gleichenhagen, J.; Grund, N.; Wagner, D.; Schwalbe, H.; Hoffknecht, B.; Metzler-Nolte, N.; Narberhaus, F.
    Membrane-binding mechanism of a bacterial phospholipid N-methyltransferase (2015), Mol. Microbiol., 95, 313-331.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
DeltaN30 truncated PmtA variant missing the first 30 amino acids, completely inactive Agrobacterium tumefaciens
F19A inactive Agrobacterium tumefaciens
K6Q/R8Q/K12Q mutant produced wild-type-like amounts of the first intermediate monomethyl-phosphatidylethanolamine (C18:1) and reduced amounts of dimethyl-phosphatidylethanolamine (C18:1) and phosphatidylcholine Agrobacterium tumefaciens
R18Q/K21Q/K28Q/K29Q mutations of the positively charged residues in the C-terminal part of the alphaA helix, do not influence polar localization Agrobacterium tumefaciens

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane enzyme attaches to the membrane via electrostatic interactions with anionic lipids, which do not serve as substrate. Increasing phosphatidylcholine concentrations trigger membrane dissociation suggesting that membrane binding of PmtA is negatively regulated by its end product phosphatidylcholine. alpha-Helical regions alphaA and alphaF contribute to membrane binding. The latter undergoes a structural transition from disordered to alpha-helical conformation in the presence of anionic lipids. The basic amino acids R8 and K12 and the hydrophobic amino acid F19 are critical for membrane binding by alphaA as well as for activity of full-length PmtA Agrobacterium tumefaciens 16020
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Organism

Organism UniProt Comment Textmining
Agrobacterium tumefaciens
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Synonyms

Synonyms Comment Organism
PmtA
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Agrobacterium tumefaciens