Crystal Structure of an ATP-Dependent DNA Ligase from Bacteriophage T7 [PDF]
The crystal structure of the ATP-dependent DNA ligase from bacteriophage T7 has been solved at 2.6 A resolution. The protein comprises two domains with a deep cleft running between them. The structure of a complex with ATP reveals that the nucleotide binding pocket is situated on the larger N-terminal domain, at the base of the cleft between the two ...
Hosahalli S. Subramanya +3 more
semanticscholar +4 more sources
Characterization of an ATP-dependent DNA ligase encoded by Haemophilus influenzae [PDF]
We report that Haemophilus influenzae encodes a 268 amino acid ATP-dependent DNA ligase. The specificity of Haemophilus DNA ligase was investigated using recombinant protein produced in Escherichia coli. The enzyme catalyzed efficient strand joining on a singly nicked DNA in the presence of magnesium and ATP (Km = 0.2 microM).
Chonghui Cheng
semanticscholar +4 more sources
Characterization of an ATP-dependent DNA ligase from the acidophilic archaeon “Ferroplasma acidarmanus” Fer1 [PDF]
Analysis of the genome of "Ferroplasma acidarmanus" Fer1, an archaeon that is an extreme acidophile, identified an open reading frame encoding a putative ATP-dependent DNA ligase, which we termed FaLig. The deduced amino acid sequence of FaLig contains 595 amino acids, with a predicted molecular mass of 67.8 kDa. "F.
Brian R. Jackson +4 more
semanticscholar +6 more sources
Characterization of an ATP-dependent DNA ligase from the thermophilic archaeon Methanobacterium thermoautotrophicum [PDF]
We report the production, purification and characterization of a DNA ligase encoded by the thermophilic archaeon Methanobacterium thermoautotrophicum. The 561 amino acid MTH: ligase catalyzed strand-joining on a singly nicked DNA in the presence of a divalent cation (magnesium, manganese or cobalt) and ATP (K(m) 1.1 microM). dATP can substitute for ATP,
Verl Sriskanda
semanticscholar +4 more sources
Characterization of an ATP-dependent DNA ligase encoded by Chlorella virus PBCV-1 [PDF]
We report that Chlorella virus PBCV-1 encodes a 298-amino-acid ATP-dependent DNA ligase. The PBCV-1 enzyme is the smallest member of the covalent nucleotidyl transferase superfamily, which includes the ATP-dependent polynucleotide ligases and the GTP-dependent RNA capping enzymes.
C. Kiong Ho +2 more
semanticscholar +4 more sources
Recombinant expression and purification of an ATP-dependent DNA ligase from Aliivibrio salmonicida [PDF]
The genome of the psychrophilic fish-pathogen Aliivibrio salmonicida encodes a putative ATP-dependent DNA ligase in addition to a housekeeping NAD-dependent enzyme. In order to study the structure and activity of the ATP dependent ligase in vitro we have undertaken its recombinant production and purification from an Escherichia coli based expression ...
Adele Williamson, Hege Lynum Pedersen
semanticscholar +5 more sources
Characterization of a Baculovirus-Encoded ATP-Dependent DNA Ligase [PDF]
ABSTRACTSequence analysis of theLymantria disparmulticapsid nucleopolyhedrovirus (LdMNPV) genome identified an open reading frame (ORF) encoding a 548-amino-acid (62-kDa) protein that showed 35% amino acid sequence identity with vaccinia virus ATP-dependent DNA ligase. Ligase homologs have not been reported from other baculoviruses.
Margot Pearson, George F Rohrmann
semanticscholar +4 more sources
Use of ATP, dATP and their α-thio derivatives to study DNA ligase adenylation [PDF]
Bacteriophage-T4 and human type I DNA ligases were found capable of self-adenylating upon exposure to both ribo- and deoxyribo-[alpha-35S]thio-ATP. However, the joining reaction does not take place in the presence of the deoxyribotriphosphates. Enzyme adenylation is reversed in all cases by an excess of PPi, but the rate of reversion is lower with thio
Alessandra Montecucco +4 more
semanticscholar +6 more sources
ATP-dependent DNA ligase fromThermococcussp. 1519 displays a new arrangement of the OB-fold domain [PDF]
DNA ligases join single-strand breaks in double-stranded DNA by catalyzing the formation of a phosphodiester bond between adjacent 5'-phosphate and 3'-hydroxyl termini. Their function is essential for maintaining genome integrity in the replication, recombination and repair of DNA. High flexibility is important for the function of DNA ligase molecules.
T. Petrova +12 more
semanticscholar +5 more sources
ATP-dependent DNA ligase fromArchaeoglobus fulgidusdisplays a tightly closed conformation [PDF]
DNA ligases join the breaks in double-stranded DNA by catalyzing the formation of a phosphodiester bond between adjacent 3'-hydroxyl and 5'-phosphate termini. They fall into two classes that require either ATP or NAD(+) as the source of an AMP group that is covalently attached to a strictly conserved lysine.
Dojin Kim +5 more
semanticscholar +5 more sources

