Structure of sodium (–)-shikimate dihydrate

Abell, C.; Allen, Frank H.; Bugg, Timothy D. H.; Doyle, Michael J.; Raithby, P. R.

doi:10.1107/s0108270188002872

Cited by 5 publications

(3 citation statements)

References 9 publications

(11 reference statements)

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“…Starting coordinates for R and S forms of the EPSP synthase tetrahedral intermediate (1, Figure 3), the R and S forms of the phosphonate intermediate analog (2, Figure 3), and an S3P-Glp bisubstrate analog (3, Figure 3) were built from the reported X-ray structure for shikimate (Abell et al, 1988) using the sketching tools within SYBYL. Starting coordinates for Glp were taken from a reported X-ray structure (Knuuttila & Knuuttila, 1979).…”

Section: Methodsmentioning

confidence: 99%

“…The 46-kDa enzyme 5-enolpyruvylshikimate-3-phosphate (EPSP) synthase catalyzes the reversible condensation of shikimate 3-phosphate (S3P) and phosphoenolpyruvate (PEP) to form EPSP in the synthesis of aromatic amino acids in plants and microorganisms (Steinrucken & Amrhein, 1984a; Anderson & Johnson, 1990). This reaction is inhibited by the commercial herbicide N -(phosphonomethyl)glycine (glyphosate or Glp), HO 3 PCH 2 NHCH 2 COOH, which, in the presence of S3P, binds to EPSP synthase (EPSPS) and forms a stable, ternary complex (Steinrucken & Amrhein, 1984b; Anderson et al, 1988a).…”

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confidence: 99%

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Ligand Geometry of the Ternary Complex of 5-Enolpyruvylshikimate-3-phosphate Synthase from Rotational-Echo Double-Resonance NMR

et al. 1996

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The 46-kDa enzyme 5-enolpyruvylshikimate-3-phosphate (EPSP) synthase catalyzes the condensation of shikimate 3-phosphate (S3P) and phosphoenolpyruvate (PEP) to form EPSP. The reaction is inhibited by N-(phosphonomethyl)glycine (Glp), which, in the presence of S3P, binds to EPSP synthase to form a stable ternary complex. As part of a solid-state NMR characterization of this structure, we have used dipolar recovery at the magic angle (DRAMA) and rotational-echo double resonance (REDOR) to determine intra- and interligand internuclear distances. DRAMA was used to determine the single 31P-31P distance, while REDOR was used to determine one 31P-15N distance and five 31P-13C distances. These experimental distances were used as restraints in molecular dynamics simulations of an S3P-Glp complex to examine the geometry of the two ligands relative to one another in the ternary complex. The simulations were compared to unrestrained simulations of the EPSP synthase tetrahedral intermediate and its phosphonate analog. The results suggest that Glp is unlikely to bind in the same fashion as PEP, a conclusion that is consistent with recent studies that have questioned the role of Glp as a transition-state or intermediate analog.

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Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

Ligand Geometry of the Ternary Complex of 5-Enolpyruvylshikimate-3-phosphate Synthase from Rotational-Echo Double-Resonance NMR

et al. 1996

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“…This pathway is of agrochemical interest as a potential target for herbicides. As part of a program designed to obtain accurate structural data for shikimates and related molecules we have recently reported the structure of sodium (-)-shikimate dihydrate (Abell, Allen, Bugg, Doyle & Raithby, 1988). We now report the structure of (--)-quinic acid.…”

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confidence: 99%