Structure of the human RECQ1 helicase reveals a putative strand-separation pin.
|Abstract||RecQ-like helicases, which include 5 members in the human genome, are important in maintaining genome integrity. We present a crystal structure of a truncated form of the human RECQ1 protein with Mg-ADP. The truncated protein is active in DNA fork unwinding but lacks other activities of the full-length enzyme: disruption of Holliday junctions and DNA strand annealing. The structure of human RECQ1 resembles that of Escherichia coli RecQ, with some ... [truncated at 450 characters in length]|
|Author||Pike, Ashley C W; Shrestha, Binesh; Popuri, Venkateswarlu; et al|
|Subject||Adenosine Diphosphate Adenosine Triphosphate Amino Acid Motifs Amino Acid Sequence Conserved Sequence DNA Escherichia coli Humans Kinetics Molecular Sequence Data Mutant Proteins Protein Binding Protein Structure, Tertiary RecQ Helicases Sequence Alignment Zinc metabolism metabolism enzymology chemistry chemistry metabolism metabolism|
Structural basis for different specificities of acyltransferases associated with the human cytosolic and mitochondrial fatty acid synthases.
|Abstract||Animals employ two systems for the de novo biosynthesis of fatty acids: a megasynthase complex in the cytosol (type I) that produces mainly palmitate, and an ensemble of freestanding enzymes in the mitochondria (type II) that produces mainly octanoyl moieties. The acyltransferases responsible for initiation of fatty acid biosynthesis in the two compartments are distinguished by their different substrate specificities: the type I enzyme transfers ... [truncated at 450 characters in length]|
|Author||Bunkoczi, Gabor; Misquitta, Stephanie; Wu, Xiaoqiu; et al|
|Subject||Acyltransferases Amino Acid Sequence Catalytic Domain Computer Simulation Crystallography, X-Ray Cytosol Fatty Acid Synthetase Complex, Type I Fatty Acid Synthetase Complex, Type II Fatty Acids Humans Mitochondria Molecular Sequence Data Mutagenesis, Site-Directed Mutant Proteins Sequence Alignment Sequence Homology, Amino Acid Substrate Specificity chemistry genetics metabolism enzymology chemistry metabolism chemistry metabolism biosynthesis enzymology metabolism genetics metabolism|
Crystal structure of the 2-oxoglutarate- and Fe(II)-dependent lysyl hydroxylase JMJD6.
|Abstract||Lysyl and prolyl hydroxylations are well-known post-translational modifications to animal and plant proteins with extracellular roles. More recent work has indicated that the hydroxylation of intracellular animal proteins may be common. JMJD6 catalyses the iron- and 2-oxoglutarate-dependent hydroxylation of lysyl residues in arginine-serine-rich domains of RNA splicing-related proteins. We report crystallographic studies on the catalytic domain o ... [truncated at 450 characters in length]|
|Author||Mantri, Monica; Krojer, Tobias; Bagg, Eleanor A; et al|
|Subject||Amino Acid Sequence Amino Acid Substitution Base Sequence Catalytic Domain Crystallography, X-Ray DNA Primers Humans Iron Jumonji Domain-Containing Histone Demethylases Ketoglutaric Acids Models, Molecular Molecular Sequence Data Mutagenesis, Site-Directed Mutant Proteins Nickel Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase Protein Folding Recombinant Proteins Sequence Homology, Amino Acid Static Electricity genetics metabolism chemistry genetics metabolism metabolism chemistry genetics metabolism metabolism chemistry genetics metabolism chemistry genetics metabolism|