1dos

STRUCTURE OF FRUCTOSE-BISPHOSPHATE ALDOLASE

spinqualitylabelsall models 1dos, resolution 1.67Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1dos is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: NH4, ZN Activity: Fructose-bisphosphate aldolase, with EC number 4.1.2.13 Resources: FirstGlance, OCA, RCSB, PDBsum 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 The molecular architecture of the Class II E. coli fructose 1,6-bisphosphate aldolase dimer was determined to 1.6 A resolution. The subunit fold corresponds to a singly wound alpha/beta-barrel with an active site located on the beta-barrel carboxyl side of each subunit. In each subunit there are two mutually exclusive zinc metal ion binding sites, 3.2 A apart; the exclusivity is mediated by a conformational transition involving side-chain rotations by chelating histidine residues. A binding site for K+ and NH4+ activators was found near the beta-barrel centre. Although Class I and Class II aldolases catalyse identical reactions, their active sites do not share common amino acid residues, are structurally dissimilar, and from sequence comparisons appear to be evolutionary distinct. Novel active site in Escherichia coli fructose 1,6-bisphosphate aldolase.,Blom NS, Tetreault S, Coulombe R, Sygusch J Nat Struct Biol. 1996 Oct;3(10):856-62. PMID:8836102 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aldolase

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