3FUA
L-FUCULOSE-1-PHOSPHATE ALDOLASE CRYSTAL FORM K
Summary for 3FUA
| Entry DOI | 10.2210/pdb3fua/pdb |
| Descriptor | L-FUCULOSE-1-PHOSPHATE ALDOLASE, ZINC ION, SULFATE ION, ... (6 entities in total) |
| Functional Keywords | class ii aldolase, zinc enzyme, lyase, lyase (aldehyde) |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 24080.38 |
| Authors | Dreyer, M.K.,Schulz, G.E. (deposition date: 1996-02-14, release date: 1996-10-14, Last modification date: 2024-06-05) |
| Primary citation | Dreyer, M.K.,Schulz, G.E. Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure. J.Mol.Biol., 259:458-466, 1996 Cited by PubMed Abstract: The structure of L-fuculose-1-phosphate aldolase in a cubic crystal form has been determined with and without the inhibitor phosphoglycolohydroxamate at 2.4 and 2.7 angstrom (1 angstrom = 0.1 nm) resolution, respectively. This inhibitor mimics the enediolate transition state of the substrate moiety dihydroxyacetone phosphate. The structures showed that dihydroxyacetone phosphate ligates the zinc ion of this metal-dependent class II aldolase with its hydroxyl and keto oxygen atoms, shifting Glu73 away from the zinc coordination sphere to a non-polar environment. At this position Glu73 accepts a proton in the initial reaction step, producing the enediolate which is then stabilized by the zinc ion. The other substrate moiety L-lactaldehyde was modeled, because no binding structure is yet available. PubMed: 8676381DOI: 10.1006/jmbi.1996.0332 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.67 Å) |
Structure validation
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