1FUA: L-Fuculose 1-Phosphate Aldolase Crystal Form T

Citation:
Abstract
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.
PDB ID: 1FUADownload
MMDB ID: 56188
PDB Deposition Date: 1996/2/14
Updated in MMDB: 2011/11
Experimental Method:
x-ray diffraction
Resolution: 1.92  Å
Similar Structures:
Biological Unit for 1FUA: tetrameric; determined by author and by software (PISA,PQS)
Molecular Components in 1FUA
Label Count Molecule
Proteins (4 molecules)
4
L-fuculose-1-phosphate Aldolase(Gene symbol: fucA)
Molecule annotation
Chemicals (16 molecules)
1
4
2
8
3
4
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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