Structure-guided mutational analysis of the nucleotidyltransferase domain of Escherichia coli NAD+-dependent DNA ligase (LigA). (Q45238566)

11 December 2017

title

Structure-guided mutational analysis of the nucleotidyltransferase domain of Escherichia coli NAD+-dependent DNA ligase (LigA). (English)

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11 December 2017

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2

Stewart Shuman

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11 December 2017

Hui Zhu

1

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11 December 2017

language of work or name

English

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publication date

24 January 2005

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Journal of Biological Chemistry

11 December 2017

published in

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11 December 2017

volume

280

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11 December 2017

issue

13

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11 December 2017

page(s)

12137-12144

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DNA ligase: structure, mechanism, and function

11 December 2017

cites work

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The NAD-dependent ligase encoded by yerG is an essential gene of Bacillus subtilis

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Biochemical and genetic analysis of the four DNA ligases of mycobacteria

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Specific and potent inhibition of NAD+-dependent DNA ligase by pyridochromanones

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Structure of the adenylation domain of an NAD+-dependent DNA ligase

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Crystal structure of NAD+-dependent DNA ligase: modular architecture and functional implications

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Crystal structure of an ATP-dependent DNA ligase from bacteriophage T7

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X-ray crystallography reveals a large conformational change during guanyl transfer by mRNA capping enzymes

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Crystal structure of eukaryotic DNA ligase-adenylate illuminates the mechanism of nick sensing and strand joining

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Structure of an mRNA capping enzyme bound to the phosphorylated carboxy-terminal domain of RNA polymerase II

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Structure and mechanism of RNA ligase

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RNA capping enzyme and DNA ligase: a superfamily of covalent nucleotidyl transferases

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Role of nucleotidyltransferase motifs I, III and IV in the catalysis of phosphodiester bond formation by Chlorella virus DNA ligase

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Role of nucleotidyl transferase motif V in strand joining by chlorella virus DNA ligase

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Mutational analysis of bacteriophage T4 RNA ligase 1. Different functional groups are required for the nucleotidyl transfer and phosphodiester bond formation steps of the ligation reaction

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Mutational analysis of the guanylyltransferase component of Mammalian mRNA capping enzyme

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Cloning and functional characterization of an NAD(+)-dependent DNA ligase from Staphylococcus aureus

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Mutational analysis of Escherichia coli DNA ligase identifies amino acids required for nick-ligation in vitro and for in vivo complementation of the growth of yeast cells deleted for CDC9 and LIG4

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Structure of the DNA ligase-adenylate intermediate: lysine (epsilon-amino)-linked adenosine monophosphoramidate

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Enzymatic characterization of a mutant of Escherichia coli with an altered DNA ligase

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Identifiers

DOI

10.1074/JBC.M413685200

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