2imo

Crystal structure of allantoate amidohydrolase from Escherichia coli at pH 4.6

spinqualitylabelsall models 2imo, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2imo is a 2 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: MSE Related: 1z2l Gene: allC_ecoli (ECOLI) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, TOPSAN Function [ALLC_ECOLI] Involved in the anaerobic utilization of allantoin. Converts allantoate to (S)-ureidoglycolate and ammonia. 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 Purine metabolism plays a major role in regulating the availability of purine nucleotides destined for nucleic acid synthesis. Allantoate amidohydrolase catalyzes the conversion of allantoate to (S)-ureidoglycolate, one of the crucial alternate steps in purine metabolism. The crystal structure of a ternary complex of allantoate amidohydrolase with its substrate allantoate and an allosteric effector, a sulfate ion, from Escherichia coli was determined to understand better the catalytic mechanism and substrate specificity. The 2.25 A resolution X-ray structure reveals an alpha/beta scaffold akin to zinc exopeptidases of the peptidase M20 family and lacks the (beta/alpha)(8)-barrel fold characteristic of the amidohydrolases. Arrangement of the substrate and the two co-catalytic zinc ions at the active site governs catalytic specificity for hydrolysis of N-carbamyl versus the peptide bond in exopeptidases. In its crystalline form, allantoate amidohydrolase adopts a relatively open conformation. However, structural analysis reveals the possibility of a significant movement of domains via rotation about two hinge regions upon allosteric effector and substrate binding resulting in a closed catalytically competent conformation by bringing the substrate allantoate closer to co-catalytic zinc ions. Two cis-prolyl peptide bonds found on either side of the dimerization domain in close proximity to the substrate and ligand-binding sites may be involved in protein folding and in preserving the integrity of the catalytic site. Structural analysis of a ternary complex of allantoate amidohydrolase from Escherichia coli reveals its mechanics.,Agarwal R, Burley SK, Swaminathan S J Mol Biol. 2007 Apr 27;368(2):450-63. Epub 2007 Feb 20. PMID:17362992 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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