1DOS
STRUCTURE OF FRUCTOSE-BISPHOSPHATE ALDOLASE
Summary for 1DOS
| Entry DOI | 10.2210/pdb1dos/pdb |
| Descriptor | ALDOLASE CLASS II, ZINC ION, AMMONIUM ION, ... (4 entities in total) |
| Functional Keywords | lyase, classii fructose 1, 6-bisphosphate aldolase, glycolysis |
| Biological source | Escherichia coli |
| Total number of polymer chains | 2 |
| Total formula weight | 78234.73 |
| Authors | Blom, N.,Tetreault, S.,Coulombe, R.,Sygusch, J. (deposition date: 1996-06-24, release date: 1997-07-07, Last modification date: 2024-02-07) |
| Primary citation | Blom, N.S.,Tetreault, S.,Coulombe, R.,Sygusch, J. Novel active site in Escherichia coli fructose 1,6-bisphosphate aldolase. Nat.Struct.Biol., 3:856-862, 1996 Cited by PubMed Abstract: 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. PubMed: 8836102DOI: 10.1038/nsb1096-856 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.67 Å) |
Structure validation
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