6EER

Structure of glycine-bound GoxA from Pseudoalteromonas luteoviolacea

Summary for 6EER

• Entry DOI: 10.2210/pdb6eer/pdb
• Related: 6BYW
• Descriptor: GoxA, MAGNESIUM ION, SODIUM ION, ... (7 entities in total)
• Functional Keywords: glycine oxidase, tryptophylquinone, unknown function
• Biological source: Pseudoalteromonas luteoviolacea DSM 6061
• Total number of polymer chains: 4
• Total formula weight: 366850.95

Authors

Yukl, E.T.,Avalos, D. (deposition date: 2018-08-15, release date: 2019-01-16, Last modification date: 2023-10-11)

Primary citation

Avalos, D.,Sabuncu, S.,Mamounis, K.J.,Davidson, V.L.,Moenne-Loccoz, P.,Yukl, E.T.
Structural and Spectroscopic Characterization of a Product Schiff Base Intermediate in the Reaction of the Quinoprotein Glycine Oxidase, GoxA.
Biochemistry, 58:706-713, 2019

PubMed Abstract: The LodA-like proteins make up a recently identified family of enzymes that rely on a cysteine tryptophylquinone cofactor for catalysis. They differ from other tryptophylquinone enzymes in that they are oxidases rather than dehydrogenases. GoxA is a member of this family that catalyzes the oxidative deamination of glycine. Our previous work with GoxA from Pseudoalteromonas luteoviolacea demonstrated that this protein forms a stable intermediate upon anaerobic incubation with glycine. The spectroscopic properties of this species were unique among those identified for tryptophylquinone enzymes characterized to date. Here we use X-ray crystallography and resonance Raman spectroscopy to identify the GoxA catalytic intermediate as a product Schiff base. Structural work additionally highlights features of the active site pocket that confer substrate specificity, intermediate stabilization, and catalytic activity. The unusual properties of GoxA are discussed within the context of the other tryptophylquinone enzymes.

PubMed: 30605596
DOI: 10.1021/acs.biochem.8b01145

Experimental method

X-RAY DIFFRACTION (1.82 Å)