9QUR

Crystal structure of gamma-Glutamyl-Methylamide Synthetase from Methylovorus mays (MmGmaS) in complex with ATPgS

This is a non-PDB format compatible entry.

Summary for 9QUR

• Entry DOI: 10.2210/pdb9qur/pdb
• Descriptor: Glutamate--methylamine ligase, PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: ligase, complex, atp-dependent
• Biological source: Methylovorus mays
• Total number of polymer chains: 6
• Total formula weight: 299128.30

Authors

Vascon, F.,Loprete, G.,Bergantino, E.,Cendron, L. (deposition date: 2025-04-11, release date: 2026-01-28)

Primary citation

Loprete, G.,Traverso, E.,Vascon, F.,Botteri, M.,Robescu, M.S.,Ubiali, D.,Cendron, L.,Morosinotto, T.,Bergantino, E.
Harnessing Photosynthetic ATP for Whole-Cell Biocatalysis in the Cyanobacterium Synechocystis.
Acs Sustain Chem Eng, 13:18667-18677, 2025

PubMed Abstract: Photosynthetic organisms use sunlight to produce ATP and NADPH powering their metabolism. Harnessing these products for driving biocatalytic reactions would enable development of clean and sustainable alternatives for chemical reactions. In this study, we present the demonstration that ATP produced from the photosynthetic process can fuel a biocatalytic transformation in the whole-cell configuration. This result was achieved by expressing in the cyanobacterium sp. PCC 6803 an ATP-dependent enzyme, the γ-glutamyl-methylamide synthetase from No. 9 (GMAS). The expressed enzyme was able to drive, in the transgenic strain, the light-driven biosynthesis of l-theanine. Consumption of ATP by the recombinant GMAS was even beneficial under strong illumination, protecting the photosynthetic electron transport from photodamage. These findings demonstrate the possibility of using photosynthetic microorganisms like as a potential platform for sunlight driven biotransformations with wide potential biocatalytic applications. In this perspective, we further present the tridimensional structure of GMAS, which explains its promiscuous activity and provides the basis for its rational evolution.

PubMed: 41199801
DOI: 10.1021/acssuschemeng.5c07236

Experimental method

X-RAY DIFFRACTION (2.65 Å)