3e74

Crystal structure of E. coli allantoinase with iron ions at the metal center

spinqualitylabelsall models 3e74, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3e74 is a 4 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FE NonStd Res: KCX, MSE Related: 3e75 Gene: allB, glxB3, ybbX, b0512, JW0500 (ECOLI) Activity: Allantoinase, with EC number 3.5.2.5 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ALLB_ECOLI] Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Allantoinase acts as a key enzyme for the biogenesis and degradation of ureides by catalyzing the conversion of (S)-allantoin into allantoate, the final step in the ureide pathway. Despite limited sequence similarity, biochemical studies of the enzyme suggested that allantoinase belongs to the amidohydrolase family. In this study, the crystal structure of allantoinase from Escherichia coli was determined at 2.1 A resolution. The enzyme consists of a homotetramer in which each monomer contains two domains: a pseudo-triosephosphate-isomerase barrel and a beta-sheet. Analogous to other enzymes in the amidohydrolase family, allantoinase retains a binuclear metal center in the active site, embedded within the barrel fold. Structural analyses demonstrated that the metal ions in the active site ligate one hydroxide and six residues that are conserved among allantoinases from other organisms. Functional analyses showed that the presence of zinc in the metal center is essential for catalysis and enantioselectivity of substrate. Both the metal center and active site residues Asn94 and Ser317 play crucial roles in dictating enzyme activity. These structural and functional features are distinctively different from those of the metal-independent allantoinase, which was very recently identified. Crystal structure of metal-dependent allantoinase from Escherichia coli.,Kim K, Kim MI, Chung J, Ahn JH, Rhee S J Mol Biol. 2009 Apr 17;387(5):1067-74. Epub 2009 Feb 24. PMID:19248789 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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