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Literature summary extracted from

  • Dalkas, G.A.; Papakyriakou, A.; Vlamis-Gardikas, A.; Spyroulias, G.A.
    Insights into the anthrax lethal factor-substrate interaction and selectivity using docking and molecular dynamics simulations (2009), Protein Sci., 18, 1774-1785.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.24.83 docking and molecular dynamics calculations to examine the anthrax lethal factor-MEK/MKK interaction along the catalytic channel up to a distance of 20 A from the zinc atom. The Zn-bound water molecule is predicted to form hydrogen bonds with the carbonyl oxygen of Ile, i.e. P1' of substrates MEK1, MKK3b, Leu, ie. P1' of substrate MKK4-1, and Leu, ie. P2 of substrate MKK6b as well as with the hydroxyl group of Thr, i.e. P2' of substrate MKK4-2. This hydrogen bond is an additional contact to the already existing polarization of the carbonyl oxygen between Zn and Glu687 carboxylate Bacillus anthracis

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.83 Bacillus anthracis
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.83 MEK1 + H2O mitogen-activated protein kinase kinase, cleavage between residues 8-9 Bacillus anthracis ?
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3.4.24.83 MEK2 + H2O mitogen-activated protein kinase kinase, cleavage between residues 10-11 Bacillus anthracis ?
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 ?
3.4.24.83 MKK3b + H2O mitogen-activated protein kinase kinase, cleavage between residues 26-27 Bacillus anthracis ?
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 ?
3.4.24.83 MKK4 + H2O mitogen-activated protein kinase kinase, cleavage between residues 45-46 and 58-59 Bacillus anthracis ?
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3.4.24.83 MKK6b + H2O mitogen-activated protein kinase kinase, cleavage between residues 14-15 Bacillus anthracis ?
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 ?
3.4.24.83 MKK7beta + H2O mitogen-activated protein kinase kinase, cleavage between residues 44-45 and 76-77 Bacillus anthracis ?
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