1E46
L-Fuculose 1-Phosphate Aldolase from Escherichia coli Mutant E73S
Summary for 1E46
| Entry DOI | 10.2210/pdb1e46/pdb |
| Related | 1DZU 1DZV 1DZW 1DZX 1DZY 1DZZ 1E47 1E48 1E49 1E4A 1E4B 1E4C 1FUA 2FUA 3FUA 4FUA |
| Descriptor | L-FUCULOSE 1-PHOSPHATE ALDOLASE, SULFATE ION, BETA-MERCAPTOETHANOL, ... (5 entities in total) |
| Functional Keywords | aldolase (class ii), bacterial l-fucose metabolism, cleavage of l-fuculose 1-phosphate to dihydroxyacetone phosphate and l-lactaldehyde, mutant structure |
| Biological source | ESCHERICHIA COLI |
| Total number of polymer chains | 1 |
| Total formula weight | 24002.89 |
| Authors | Joerger, A.C.,Schulz, G.E. (deposition date: 2000-06-30, release date: 2000-11-06, Last modification date: 2019-01-30) |
| Primary citation | Joerger, A.C.,Mueller-Dieckmann, C.,Schulz, G.E. Structures of L-Fuculose-1-Phosphate Aldolase Mutants Outlining Motions During Catalysis J.Mol.Biol., 303:531-, 2000 Cited by PubMed Abstract: The crystal structures of l-fuculose-1-phosphate aldolase (FucA) with and without a ligated analogue of dihydroxyacetone phosphate (DHAP) and of a number of active center mutants have resulted in a model of the catalytic mechanism. This model has now been confirmed by structural analyses of further mutations at the zinc coordination sphere and at the phosphate site. In addition, these mutants have revealed new aspects of the catalysis: the hydroxyl group of Tyr113' (from a neighboring subunit), which sits just outside the zinc coordination sphere, steers DHAP towards a productive binding mode at the zinc ion; Glu73 contacts zinc in between the two ligand positions intended for the DHAP oxygen atoms and thus avoids blocking of these positions by a tetrahedrally coordinated hydroxy ion; the FucA polypeptide does not assume its minimum energy state but oscillates between two states of elevated energy as demonstrated by a mutant in a minimum energy state. The back and forth motion involves a mobile loop connecting the phosphate site with intersubunit motions and thus with the Brownian motion of the solvent. The phosphate group is bound strongly at a given distance to the zinc ion, which prevents the formation of too tight a DHAP:zinc complex. This observation explains our failure to find mutants that accept phosphate-free substitutes for DHAP. The FucA zinc coordination sphere is compared with that of carbonic anhydrase. PubMed: 11054289DOI: 10.1006/JMBI.2000.4153 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.55 Å) |
Structure validation
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