6c6g

An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex.

spinqualitylabelsall models 6c6g, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6c6g is a 4 chain structure with sequence from Pseudomonas sp. ADP. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Ligands: CA, SVV Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ATZE_PSESD Publication Abstract from PubMed Cyanuric acid is a metabolic intermediate of s-triazines, such as atrazine (a common herbicide) and melamine (used in resins and plastics). Cyanuric acid is mineralized to ammonia and carbon dioxide by the soil bacterium Pseudomonas sp. strain ADP via three hydrolytic enzymes (AtzD, AtzE, and AtzF). Here, we report the purification and biochemical and structural characterization of AtzE. Contrary to previous reports, we found that AtzE is not a biuret amidohydrolase, but instead catalyzes the hydrolytic deamination of 1-carboxybiuret. X-ray crystal structures of apo AtzE and AtzE bound with the suicide inhibitor phenyl phosphorodiamidate revealed that the AtzE enzyme complex consists of two independent molecules in the asymmetric unit. We also show that AtzE forms an alpha2beta2 heterotetramer with a hitherto unidentified 68-amino-acid-long protein (AtzG) encoded in the cyanuric acid mineralization operon from Pseudomonas sp. strain ADP. Moreover, we observed that AtzG is essential for the production of soluble, active AtzE and that this obligate interaction is a vestige of their shared evolutionary origin. We propose that AtzEG was likely recruited into the cyanuric acid-mineralizing pathway from an ancestral glutamine transamidosome that required protein-protein interactions to enforce the exclusion of solvent from the transamidation reaction. An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme.,Esquirol L, Peat TS, Wilding M, Liu JW, French NG, Hartley CJ, Onagi H, Nebl T, Easton CJ, Newman J, Scott C J Biol Chem. 2018 Mar 9. pii: RA118.001996. doi: 10.1074/jbc.RA118.001996. PMID:29523689 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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