6eer | pdb_00006eer

Structure of glycine-bound GoxA from Pseudoalteromonas luteoviolacea

spinqualitylabelsall models 6eer, resolution 1.82Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6eer is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: EDO, MG, NA, PEG, PGE NonStd Res: TNQ Related: 6byw Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The LodA-like proteins are a recently identified family of enzymes that rely on a cysteine tryptophylquinone (CTQ)1 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 luteoviolaceae 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. Structural and spectroscopic characterization of a product Schiff-base intermediate in the reaction of the quinoprotein glycine oxidase, GoxA.,Avalos D, Sabuncu S, Mamounis KJ, Davidson VL, Moenne-Loccoz P, Yukl ET Biochemistry. 2019 Jan 3. doi: 10.1021/acs.biochem.8b01145. PMID:30605596 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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