Summary for 4BVQ
| Entry DOI | 10.2210/pdb4bvq/pdb |
| Related | 4BVR 4BVS 4BVT |
| Descriptor | CYANURIC ACID AMIDOHYDROLASE, PHOSPHATE ION, MAGNESIUM ION, ... (5 entities in total) |
| Functional Keywords | hydrolase, amidase, cyanuric acid |
| Biological source | PSEUDOMONAS SP. ADP |
| Total number of polymer chains | 2 |
| Total formula weight | 81500.34 |
| Authors | Peat, T.S.,Balotra, S.,Wilding, M.,French, N.G.,Briggs, L.J.,Panjikar, S.,Cowieson, N.,Newman, J.,Scott, C. (deposition date: 2013-06-28, release date: 2013-07-17, Last modification date: 2024-05-08) |
| Primary citation | Peat, T.S.,Balotra, S.,Wilding, M.,French, N.G.,Briggs, L.J.,Panjikar, S.,Cowieson, N.,Newman, J.,Scott, C. Cyanuric Acid Hydrolase: Evolutionary Innovation by Structural Concatenation. Mol.Microbiol., 88:1149-, 2013 Cited by PubMed Abstract: The cyanuric acid hydrolase, AtzD, is the founding member of a newly identified family of ring-opening amidases. We report the first X-ray structure for this family, which is a novel fold (termed the 'Toblerone' fold) that likely evolved via the concatenation of monomers of the trimeric YjgF superfamily and the acquisition of a metal binding site. Structures of AtzD with bound substrate (cyanuric acid) and inhibitors (phosphate, barbituric acid and melamine), along with mutagenesis studies, allowed the identification of the active site. The AtzD monomer, active site and substrate all possess threefold rotational symmetry, to the extent that the active site possesses three potential Ser-Lys catalytic dyads. A single catalytic dyad (Ser85-Lys42) is hypothesized, based on biochemical evidence and crystallographic data. A plausible catalytic mechanism based on these observations is also presented. A comparison with a homology model of the related barbiturase, Bar, was used to infer the active-site residues responsible for substrate specificity, and the phylogeny of the 68 AtzD-like enzymes in the database were analysed in light of this structure-function relationship. PubMed: 23651355DOI: 10.1111/MMI.12249 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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