Results 1 to 10 of about 74,558 (177)

Bacteriophage origin of some minimal ATP-dependent DNA ligases: a new structure from Burkholderia pseudomallei with striking similarity to Chlorella virus ligase [PDF]

open access: goldScientific Reports, 2021
DNA ligases, the enzymes responsible for joining breaks in the phosphodiester backbone of DNA during replication and repair, vary considerably in size and structure.
Jolyn Pan   +4 more
doaj   +8 more sources

A role for the ATP-dependent DNA ligase lig E of Neisseria gonorrhoeae in biofilm formation [PDF]

open access: goldBMC Microbiology
Background The ATP-dependent DNA ligase Lig E is present as an accessory DNA ligase in numerous proteobacterial genomes, including many disease-causing species.
Jolyn Pan   +4 more
doaj   +3 more sources

Crystal Structure of an ATP-Dependent DNA Ligase from Bacteriophage T7 [PDF]

open access: bronzeCell, 1996
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 ...
Stephen R. Ashford   +3 more
openaire   +5 more sources

ATP-dependent DNA ligases. [PDF]

open access: bronzeGenome biology, 2002
By catalyzing the joining of breaks in the phosphodiester backbone of duplex DNA, DNA ligases play a vital role in the diverse processes of DNA replication, recombination and repair. Three related classes of ATP-dependent DNA ligase are readily apparent in eukaryotic cells.
Stuart A. MacNeill, Ina V. Martin
openaire   +4 more sources

Characterization of an ATP-dependent DNA ligase from the thermophilic archaeon Methanobacterium thermoautotrophicum [PDF]

open access: bronzeNucleic Acids Research, 2000
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,
Jerard Hurwitz   +3 more
openaire   +4 more sources

A role for the ATP-dependent DNA ligase Lig E of Neisseria gonorrhoeae in biofilm formation [PDF]

open access: green, 2023
Abstract The ATP-dependent DNA ligase Lig E is present as an accessory DNA ligase in numerous proteobacterial genomes, including many disease-causing species. Here we have constructed a genomic Lig E knock-out in the obligate human pathogen Neisseria gonorrhoeae and characterised its growth and infection characteristics.
Jolyn Pan   +2 more
  +7 more sources

Characterization of a Baculovirus-Encoded ATP-Dependent DNA Ligase [PDF]

open access: bronzeJournal of Virology, 1998
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 N. Pearson, George F. Rohrmann
openaire   +4 more sources

T4 DNA ligase structure reveals a prototypical ATP-dependent ligase with a unique mode of sliding clamp interaction [PDF]

open access: goldNucleic Acids Research, 2018
DNA ligases play essential roles in DNA replication and repair. Bacteriophage T4 DNA ligase is the first ATP-dependent ligase enzyme to be discovered and is widely used in molecular biology, but its structure remained unknown. Our crystal structure of T4 DNA ligase bound to DNA shows a compact α-helical DNA-binding domain (DBD), nucleotidyl-transferase
Ke Shi   +11 more
openaire   +4 more sources

Enzyme–adenylate structure of a bacterial ATP-dependent DNA ligase with a minimized DNA-binding surface [PDF]

open access: hybridActa Crystallographica Section D Biological Crystallography, 2014
DNA ligases are a structurally diverse class of enzymes which share a common catalytic core and seal breaks in the phosphodiester backbone of double-stranded DNAviaan adenylated intermediate. Here, the structure and activity of a recombinantly produced ATP-dependent DNA ligase from the bacteriumPsychromonassp. strain SP041 is described.
Williamson, Adele Kim   +2 more
openaire   +5 more sources

A Primer-dependent Polymerase Function of Pseudomonas aeruginosa ATP-dependent DNA Ligase (LigD) [PDF]

open access: hybridJournal of Biological Chemistry, 2005
Pseudomonas aeruginosa encodes two putative DNA ligases: a classical NAD(+)-dependent DNA ligase (LigA) plus an ATP-dependent DNA ligase (LigD). LigD exemplifies a family of bacterial proteins that consist of a ligase domain fused to flanking domains that resemble nucleases and/or polymerases. Here we purify LigD and show that it possesses an intrinsic
Hui Zhu, Stewart Shuman
openaire   +5 more sources

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