5HUC

DAHP synthase from Corynebacterium glutamicum

5HUC の概要

• エントリーDOI: 10.2210/pdb5huc/pdb
• 分子名称: 3-Deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthase, MANGANESE (II) ION, PHOSPHOENOLPYRUVATE, ... (7 entities in total)
• 機能のキーワード: dahp synthase, shikimate pathway, transferase
• 由来する生物種: Corynebacterium glutamicum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 53122.06

構造登録者

Burschowsky, D.,Heim, J.B.,Thorbjoernsrud, H.V.,Krengel, U. (登録日: 2016-01-27, 公開日: 2017-08-02, 最終更新日: 2024-01-10)

主引用文献

Burschowsky, D.,Thorbjornsrud, H.V.,Heim, J.B.,Fahrig-Kamarauskaite, J.R.,Wurth-Roderer, K.,Kast, P.,Krengel, U.
Inter-Enzyme Allosteric Regulation of Chorismate Mutase in Corynebacterium glutamicum: Structural Basis of Feedback Activation by Trp.
Biochemistry, 57:557-573, 2018

PubMed Abstract: Corynebacterium glutamicum is widely used for the industrial production of amino acids, nucleotides, and vitamins. The shikimate pathway enzymes DAHP synthase (CgDS, Cg2391) and chorismate mutase (CgCM, Cgl0853) play a key role in the biosynthesis of aromatic compounds. Here we show that CgCM requires the formation of a complex with CgDS to achieve full activity, and that both CgCM and CgDS are feedback regulated by aromatic amino acids binding to CgDS. Kinetic analysis showed that Phe and Tyr inhibit CgCM activity by inter-enzyme allostery, whereas binding of Trp to CgDS strongly activates CgCM. Mechanistic insights were gained from crystal structures of the CgCM homodimer, tetrameric CgDS, and the heterooctameric CgCM-CgDS complex, refined to 1.1, 2.5, and 2.2 Å resolution, respectively. Structural details from the allosteric binding sites reveal that DAHP synthase is recruited as the dominant regulatory platform to control the shikimate pathway, similar to the corresponding enzyme complex from Mycobacterium tuberculosis.

PubMed: 29178787
DOI: 10.1021/acs.biochem.7b01018

実験手法

X-RAY DIFFRACTION (2.45 Å)