4iss | pdb_00004iss

SeMet-substituted Kluyveromyces lactis Allophanate Hydrolase

spinqualitylabelsall models 4iss, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4iss is a 2 chain structure with sequence from Kluyveromyces lactis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.5Å Ligands: GOL, MSE, TAR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Allophanate hydrolase (AH) converts allophanate to ammonium and carbon dioxide. It is conserved in many organisms, and is essential for their utilization of urea as the nitrogen source. It also has important functions in a newly discovered eukaryotic pyrimidine nucleic acid precursor degradation pathway, the yeast-hyphal transition that several pathogens utilize to escape the host defense, and an s-triazine herbicides degradation pathway recently emerged in many soil bacteria. We have determined the crystal structure of the Kluyveromyces lactis AH. Together with structure directed functional studies, we demonstrate that its N and C domains catalyze a two-step reaction, and contribute to maintaining a dimeric form of the enzyme, required for their optimal activities. Our studies also brought molecular insights into their catalytic mechanism. Interestingly, we found that the C domain probably catalyzes a novel form of decarboxylation reaction, which might expand the knowledge of this common reaction in biological systems. Structure and Function of Allophanate Hydrolase.,Fan C, Li Z, Yin H, Xiang S J Biol Chem. 2013 Jun 10. PMID:23754281 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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