title: Crystal structure of enolase from Drosophila melanogaster.
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 Å resolution 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.
authors.affiliation: College of Chemical Engineering, Qingdao University of Science and Technology, Qingdao, Shandong 266042, People's Republic of China.
authors.forename: Congcong
authors.initials: C
authors.lastname: Sun
authors.affiliation: Jianghuai College, Anhui University, Hefei, Anhui 230039, People's Republic of China.
authors.forename: Baokui
authors.initials: B
authors.lastname: Xu
authors.affiliation: College of Chemical Engineering, Qingdao University of Science and Technology, Qingdao, Shandong 266042, People's Republic of China.
authors.forename: Xueyan
authors.initials: X
authors.lastname: Liu
authors.affiliation: Laboratory for TCM Immunopharmacology and Molecular Biology, Institute of Basic Medicine, Shandong Academy of Medical Sciences, 18877 Jingshi Road, Jinan, Shandong 250062, People's Republic of China.
authors.forename: Zhen
authors.initials: Z
authors.lastname: Zhang
authors.affiliation: College of Chemical Engineering, Qingdao University of Science and Technology, Qingdao, Shandong 266042, People's Republic of China.
authors.forename: Zhongliang
authors.initials: Z
authors.lastname: Su
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D020134:Catalytic Domain; D003001:Cloning, Molecular; D017124:Conserved Sequence; D018360:Crystallography, X-Ray; D029721:Drosophila Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D004331:Drosophila melanogaster / Q000737:chemistry* / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D015870:Gene Expression; D005822:Genetic Vectors / Q000737:chemistry / Q000378:metabolism; D005988:Glyceric Acids / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D010751:Phosphopyruvate Hydratase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011485:Protein Binding; D000072756:Protein Conformation, alpha-Helical; D000072757:Protein Conformation, beta-Strand; D054730:Protein Interaction Domains and Motifs; D055503:Protein Multimerization; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D013379:Substrate Specificity
chemical_list: D029721:Drosophila Proteins; D005988:Glyceric Acids; D011994:Recombinant Proteins; C008885:2-phosphoglycerate; D010751:Phosphopyruvate Hydratase
keywords: Drosophila melanogaster; active site; crystal structure; dimerization; enolase; glycolysis