J Mol Biol. 1993 Jun 5;231(3):549-53.

The spatial structure of the class II L-fuculose-1-phosphate aldolase from Escherichia coli.

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Institut für Organische Chemie und Biochemie, Albert-Ludwigs-Universität, Freiburg im Breisgau, Germany.

Abstract

The three-dimensional structure of L-fuculose-1-phosphate aldolase (FucA) from Escherichia coli was determined by X-ray crystallography at a resolution of 2.13 A. The enzyme is a homotetramer with an M(r) of 23,775 per subunit. Since its activity depends on the presence of metal ions (Zn2+) the enzyme belongs to the class II aldolases. As expected from amino acid sequence comparisons, this first structure of a class II aldolase shows no similarity to the known structures of class I aldolases. It has some unusual features concerning the overall chain fold, the quaternary structure, and the co-ordination of the catalytically active zinc ion. A sequence comparison with the data bank indicated that the middle domain of the enzyme L-ribulose-5-phosphate-4-epimerase is homologous to FucA and may contain an active-center metal ion.

PMID:: 8515438; [PubMed - indexed for MEDLINE]

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Cited by 6 PubMed Central articles

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Structures reported by this article

L-Fuculose-1-Phosphate Aldolase From Escherichia Coli Mutant E214a

PDB: 1DZY

Source: Escherichia coli

Method: X-Ray Diffraction

Resolution: 2.44 Å

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