title: ATP-dependent DNA ligase from Archaeoglobus fulgidus displays a tightly closed conformation.
abstract: 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. Conformational flexibility is essential for the function of multi-domain DNA ligases because they must undergo large conformational changes involving domain rearrangements during the course of the reaction. In the absence of the nicked DNA substrate, both open and closed conformations have been observed for the ATP-dependent DNA ligases from Sulfolobus solfataricus and Pyrococcus furiosus. Here, the crystal structure of an ATP-dependent DNA ligase from Archaeoglobus fulgidus has been determined in the DNA-unbound unadenylated state. It resembles the closed conformation of P. furiosus DNA ligase but was even more closed, thus enhancing our understanding of the conformational variability of these enzymes.
authors.affiliation: Department of Chemistry, College of Natural Sciences, Seoul National University, Seoul 151 742, Republic of Korea.
authors.forename: Do Jin
authors.initials: DJ
authors.lastname: Kim
authors.forename: Olesya
authors.initials: O
authors.lastname: Kim
authors.forename: Hyeon Woo
authors.initials: HW
authors.lastname: Kim
authors.forename: Hyoun Sook
authors.initials: HS
authors.lastname: Kim
authors.forename: Sang Jae
authors.initials: SJ
authors.lastname: Lee
authors.forename: Se Won
authors.initials: SW
authors.lastname: Suh
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D019843:Archaeal Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D019611:Archaeoglobus fulgidus / Q000235:genetics / Q000378:metabolism*; D001665:Binding Sites / Q000235:genetics; D017124:Conserved Sequence; D000072481:DNA Ligase ATP; D011088:DNA Ligases / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism*; D019641:DNA, Archaeal / Q000737:chemistry* / Q000378:metabolism; D003625:Data Collection; D004926:Escherichia coli / Q000235:genetics; D006860:Hydrogen Bonding; D008958:Models, Molecular; D008968:Molecular Conformation; D008969:Molecular Sequence Data; D010710:Phosphates / Q000737:chemistry; D011485:Protein Binding / Q000235:genetics; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D013223:Statistics as Topic; D013696:Temperature; D014867:Water / Q000737:chemistry
chemical_list: D019843:Archaeal Proteins; D019641:DNA, Archaeal; D010710:Phosphates; D011994:Recombinant Proteins; D014867:Water; D000255:Adenosine Triphosphate; D011088:DNA Ligases; D000072481:DNA Ligase ATP