2AAY

EPSP synthase liganded with shikimate and glyphosate

Summary for 2AAY

• Entry DOI: 10.2210/pdb2aay/pdb
• Related: 1G6S 1G6T 1MI4 1Q36 1X8R 1X8T
• Descriptor: 3-phosphoshikimate 1-carboxyvinyltransferase, (3R,4S,5R)-3,4,5-TRIHYDROXYCYCLOHEX-1-ENE-1-CARBOXYLIC ACID, GLYPHOSATE, ... (5 entities in total)
• Functional Keywords: inside-out alpha/beta barrel, transferase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm : P0A6D3
• Total number of polymer chains: 1
• Total formula weight: 46900.07

Authors

Priestman, M.A.,Healy, M.L.,Funke, T.,Becker, A. (deposition date: 2005-07-14, release date: 2006-02-14, Last modification date: 2023-08-23)

Primary citation

Priestman, M.A.,Healy, M.L.,Funke, T.,Becker, A.
Molecular basis for the glyphosate-insensitivity of the reaction of 5-enolpyruvylshikimate 3-phosphate synthase with shikimate.
Febs Lett., 579:5773-5780, 2005

PubMed Abstract: The shikimate pathway enzyme 5-enolpyruvyl shikimate-3-phosphate synthase (EPSP synthase) has received attention in the past because it is the target of the broad-spectrum herbicide glyphosate. The natural substrate of EPSP synthase is shikimate-3-phosphate. However, this enzyme can also utilize shikimate as substrate. Remarkably, this reaction is insensitive to inhibition by glyphosate. Crystallographic analysis of EPSP synthase from Escherichia coli, in complex with shikimate/glyphosate at 1.5 Angstroms resolution, revealed that binding of shikimate induces changes around the backbone of the active site, which in turn impact the efficient binding of glyphosate. The implications from these findings with respect to the design of novel glyphosate-insensitive EPSP synthase enzymes are discussed.

PubMed: 16225867
DOI: 10.1016/j.febslet.2005.09.066

Experimental method

X-RAY DIFFRACTION (1.55 Å)