5BUF

2.37 Angstrom Structure of EPSP Synthase from acinetobacter baumannii

5BUF の概要

• エントリーDOI: 10.2210/pdb5buf/pdb
• 分子名称: 3-phosphoshikimate 1-carboxyvinyltransferase, CHLORIDE ION (3 entities in total)
• 機能のキーワード: shikimate pathway, epsp synthase, transferase
• 由来する生物種: Acinetobacter baumannii
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 96830.08

構造登録者

Sutton, K.A.,Schultz, L.W.,Breen, J.,Graham, J.,Umland, T.C. (登録日: 2015-06-03, 公開日: 2016-02-17, 最終更新日: 2023-09-27)

主引用文献

Sutton, K.A.,Breen, J.,Russo, T.A.,Schultz, L.W.,Umland, T.C.
Crystal structure of 5-enolpyruvylshikimate-3-phosphate (EPSP) synthase from the ESKAPE pathogen Acinetobacter baumannii.
Acta Crystallogr.,Sect.F, 72:179-187, 2016

PubMed Abstract: The enzyme 5-enolpyruvylshikimate-3-phosphate (EPSP) synthase catalyzes the sixth step of the seven-step shikimate pathway. Chorismate, the product of the pathway, is a precursor for the biosynthesis of aromatic amino acids, siderophores and metabolites such as folate, ubiquinone and vitamin K. The shikimate pathway is present in bacteria, fungi, algae, plants and apicomplexan parasites, but is absent in humans. The EPSP synthase enzyme produces 5-enolpyruvylshikimate 3-phosphate and phosphate from phosphoenolpyruvate and shikimate 3-phosphate via a transferase reaction, and is the target of the herbicide glyphosate. The Acinetobacter baumannii gene encoding EPSP synthase, aroA, has previously been demonstrated to be essential during host infection for the growth and survival of this clinically important drug-resistant ESKAPE pathogen. Prephenate dehydrogenase is also encoded by the bifunctional A. baumannii aroA gene, but its activity is dependent upon EPSP synthase since it operates downstream of the shikimate pathway. As part of an effort to evaluate new antimicrobial targets, recombinant A. baumannii EPSP (AbEPSP) synthase, comprising residues Ala301-Gln756 of the aroA gene product, was overexpressed in Escherichia coli, purified and crystallized. The crystal structure, determined to 2.37 Å resolution, is described in the context of a potential antimicrobial target and in comparison to EPSP synthases that are resistant or sensitive to the herbicide glyphosate.

PubMed: 26919521
DOI: 10.1107/S2053230X16001114

実験手法

X-RAY DIFFRACTION (2.37 Å)