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Acta Crystallogr F Struct Biol Commun ; 73(Pt 4): 228-234, 2017 04 01.
Article in English | MEDLINE | ID: mdl-28368282

ABSTRACT

Enolase is an important enzyme in glycolysis and various biological processes. Its dysfunction is closely associated with diseases. Here, the enolase from Drosophila melanogaster (DmENO) was purified and crystallized. A crystal of DmENO diffracted to 2.0 Šresolution and belonged to space group R32. The structure was solved by molecular replacement. Like most enolases, DmENO forms a homodimer with conserved residues in the dimer interface. DmENO possesses an open conformation in this structure and contains conserved elements for catalytic activity. This work provides a structural basis for further functional and evolutionary studies of enolase.


Subject(s)
Drosophila Proteins/chemistry , Drosophila melanogaster/chemistry , Glyceric Acids/chemistry , Phosphopyruvate Hydratase/chemistry , Amino Acid Sequence , Animals , Catalytic Domain , Cloning, Molecular , Conserved Sequence , Crystallography, X-Ray , Drosophila Proteins/genetics , Drosophila Proteins/metabolism , Drosophila melanogaster/metabolism , Escherichia coli/genetics , Escherichia coli/metabolism , Gene Expression , Genetic Vectors/chemistry , Genetic Vectors/metabolism , Glyceric Acids/metabolism , Models, Molecular , Phosphopyruvate Hydratase/genetics , Phosphopyruvate Hydratase/metabolism , Protein Binding , Protein Conformation, alpha-Helical , Protein Conformation, beta-Strand , Protein Interaction Domains and Motifs , Protein Multimerization , Recombinant Proteins/chemistry , Recombinant Proteins/genetics , Recombinant Proteins/metabolism , Substrate Specificity
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