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2fua
From Proteopedia
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L-FUCULOSE 1-PHOSPHATE ALDOLASE CRYSTAL FORM T WITH COBALT
Overview
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, ... [(full description)]
About this Structure
2FUA is a [Single protein] structure of sequence from [Escherichia coli] with CO, SO4 and BME as [ligands]. Active as [L-fuculose-phosphate aldolase], with EC number [4.1.2.17]. Structure known Active Sites: ACT and PBS. Full crystallographic information is available from [OCA].
Reference
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
Page seeded by OCA on Tue Oct 30 17:14:53 2007
