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Literature summary for 1.5.1.3 extracted from

  • Wan, Q.; Bennett, B.C.; Wymore, T.; Li, Z.; Wilson, M.A.; Brooks, C.L.; Langan, P.; Kovalevsky, A.; Dealwis, C.G.
    Capturing the catalytic proton of dihydrofolate reductase Implications for general acid-Base catalysis (2021), ACS Catal., 11, 5873-5884 .
    View publication on PubMedView publication on EuropePMC
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Crystallization (Commentary)

Crystallization (Comment) Organism
2.1 A resolution neutron structure of a pseudo-Michaelis complex determined at acidic pH, direct observation of the catalytic proton and its parent solvent molecule Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0ABQ4
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General Information

General Information Comment Organism
physiological function for mechanism, dynamics are crucial for solvent entry and protonation of substrate. The mechanism invokes the release of a sole proton from a hydronium (H3O+) ion, its pathway through a narrow channel that sterically hinders the passage of water, and the ultimate protonation of DHF at the N5 atom. DOD47 is the catalytic water that promotes protonation of the N5 atom in DHF. The deuteron, modeled into the nuclear difference density peak in the active site, possibly forms a low-barrier hydrogen bond with the oxygen atom of DOD47 and is positioned between the Met20 side chain and the DOD47 so as to define a pathway that could lead to protonation of N5 by the deuteron Escherichia coli