1fua
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L-FUCULOSE 1-PHOSPHATE ALDOLASE CRYSTAL FORM T
OverviewOverview
The structure of the class II zinc-ion dependent L-fuculose-1-phosphate, aldolase from Escherichia coli in its tetragonal crystal form has been, established at 1.92 A resolution. The homotetrameric enzyme has a, molecular mass of 4 x 24 kDa and follows C(4) symmetry. The structure, model is exactly symmetrical, which contradicts an observed birefringence, anomaly of the crystals. The four catalytic centers are located in deep, clefts at the interfaces of adjacent subunits. The zinc ion is coordinated, by three histidines and one glutamate in an almost tetrahedral, arrangement. In contrast to numerous other catalytically competent zinc, ions, there is no water molecule in the ligand sphere. Replacement of zinc, by a cobalt ion caused only small structural changes. A search through the, Protein Data Bank indicated that the chain fold is novel. Sequence, homology searches revealed a significant similarity to the bacterial, L-ribulose-5-phosphate 4-epimerase.
About this StructureAbout this Structure
1FUA is a Single protein structure of sequence from Escherichia coli with ZN, SO4 and BME as ligands. Active as L-fuculose-phosphate aldolase, with EC number 4.1.2.17 Known structural/functional Sites: and . Full crystallographic information is available from OCA.
ReferenceReference
Refined high-resolution structure of the metal-ion dependent L-fuculose-1-phosphate aldolase (class II) from Escherichia coli., Dreyer MK, Schulz GE, Acta Crystallogr D Biol Crystallogr. 1996 Nov 1;52(Pt 6):1082-91. PMID:15299567
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