5bk6

Structural and biochemical characterization of a non-canonical biuret hydrolase (BiuH) from the cyanuric acid catabolism pathway of Rhizobium leguminasorum bv. viciae 3841

spinqualitylabelsall models 5bk6, resolution 1.59Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5bk6 is a 4 chain structure with sequence from Rhizobium leguminosarum bv. viciae 3841. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.59Å Ligands: BTB, GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function BIUH_RHIL3 Involved in the degradation of cyanuric acid, an intermediate in the degradation of s-triazide herbicides such as atrazine (PubMed:21897878). Catalyzes the hydrolysis of biuret to urea-1-carboxylate (allophanate) and ammonia (PubMed:21897878, PubMed:29425231). The substrate, biuret, is formed by the spontaneous decarboxylation of carboxybiuret (PubMed:21897878). Publication Abstract from PubMed Biuret deamination is an essential step in cyanuric acid mineralization. In the well-studied atrazine degrading bacterium Pseudomonas sp. strain ADP, the amidase AtzE catalyzes this step. However, Rhizobium leguminosarum bv. viciae 3841 uses an unrelated cysteine hydrolase, BiuH, instead. Herein, structures of BiuH, BiuH with bound inhibitor and variants of BiuH are reported. The substrate is bound in the active site by a hydrogen bonding network that imparts high substrate specificity. The structure of the inactive Cys175Ser BiuH variant with substrate bound in the active site revealed that an active site cysteine (Cys175), aspartic acid (Asp36) and lysine (Lys142) form a catalytic triad, which is consistent with biochemical studies of BiuH variants. Finally, molecular dynamics simulations highlighted the presence of three channels from the active site to the enzyme surface: a persistent tunnel gated by residues Val218 and Gln215 forming a potential substrate channel and two smaller channels formed by Val28 and a mobile loop (including residues Phe41, Tyr47 and Met51) that may serve as channels for co-product (ammonia) or co-substrate (water). Structural and biochemical characterization of the biuret hydrolase (BiuH) from the cyanuric acid catabolism pathway of Rhizobium leguminasorum bv. viciae 3841.,Esquirol L, Peat TS, Wilding M, Lucent D, French NG, Hartley CJ, Newman J, Scott C PLoS One. 2018 Feb 9;13(2):e0192736. doi: 10.1371/journal.pone.0192736., eCollection 2018. PMID:29425231 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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