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Literature summary for 2.4.1.336 extracted from

  • Ge, C.; Gomez-Llobregat, J.; Skwark, M.J.; Ruysschaert, J.M.; Wieslander, A.; Linden, M.
    Membrane remodeling capacity of a vesicle-inducing glycosyltransferase (2014), FEBS J., 281, 3667-3684.
    View publication on PubMed
Search for more literature for 2.4.1.336

Crystallization (Commentary)

Crystallization (Comment) Organism
structural model displays the characteristic double Rossmann fold of the GT-B superfamily, with the active site located in the cleft between the two domains. The C-terminal tail stretches back to and interacts with the N domain, perhaps acting as a tether that maintains close contacts between the two domains Acholeplasma laidlawii

Protein Variants

Protein Variants Comment Organism
K67A/R70A mutation in the binding alpha helix, activity is dramatically reduced or even abolished, mutant is able to generate internal vesicles Acholeplasma laidlawii
K67A/R70A/R83A/K84A mutation in the binding alpha helix, activity is dramatically reduced or even abolished, mutant is able to generate internal vesicles Acholeplasma laidlawii
K76A/R77A mutation in the binding alpha helix, activity is dramatically reduced or even abolished, mutant is able to generate internal vesicles Acholeplasma laidlawii
L62A/V63A/V66A mutation in the binding alpha helix, activity is dramatically reduced or even abolished, mutant is able to generate internal vesicles Acholeplasma laidlawii
additional information deletion of 9, 19 or 29 amino acids of the C-terminal tail destroys the activity in vitro. The ability to generate internal vesicles is dirupted in mutants lacking 19 and 29 amino acids Acholeplasma laidlawii
R63A/K64A mutation in the binding alpha helix, activity is dramatically reduced or even abolished, mutant is able to generate internal vesicles Acholeplasma laidlawii
R80A/K81A mutation in the binding alpha helix, mutant is active and able to generate internal vesicles. Acholeplasma laidlawii
R83A/K84A mutation in the binding alpha helix, activity is dramatically reduced or even abolished, mutant is able to generate internal vesicles Acholeplasma laidlawii
R83A/K84A mutation in the binding alpha helix, mutant is active and able to generate internal vesicles Acholeplasma laidlawii

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane enzyme binds to the membrane in a fairly upright manner, mainly by residues in the N-terminal domain, and in a way that induces local enrichment of anionic lipids and a local curvature deformation Acholeplasma laidlawii 16020
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Organism

Organism UniProt Comment Textmining
Acholeplasma laidlawii Q93P60
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General Information

General Information Comment Organism
physiological function enzyme binds to the membrane in a fairly upright manner, mainly by residues in the N-terminal domain, and in a way that induces local enrichment of anionic lipids and a local curvature deformation. Several MGS variants resulting from substitution of residues in the membrane anchoring segment are still able to generate vesicles when heterologously expressed in Escherichia coli, regardless of enzymatic activity Acholeplasma laidlawii