Crystal structure of an ATP-dependent DNA ligase from bacteriophage T7.
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 domains of the enzyme. Comparison of the overall domain structure with that of DNA methyltransferases, coupled with other evidence, suggests that DNA also binds in this cleft. Since this structure is the first of the nucleotidyltransferase superfamily, which includes the eukaryotic mRNA capping enzymes, the relationship between the structure of DNA ligase and that of other nucleotidyltransferases is also discussed.
Subramanya
H S
HS
Laboratory of Molecular Biophysics, University of Oxford, United Kingdom.
Doherty
A J
AJ
Ashford
S R
SR
Wigley
D B
DB
D000255:Adenosine Triphosphate / Q000378:metabolism / Q000502:physiology; D017123:Bacteriophage T7 / Q000201:enzymology* / Q000378:metabolism; D001665:Binding Sites / Q000502:physiology; D003461:Crystallography; D011088:DNA Ligases / Q000737:chemistry* / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000502:physiology; D007091:Image Processing, Computer-Assisted; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009713:Nucleotidyltransferases / Q000737:chemistry; D011487:Protein Conformation; D017510:Protein Folding; D017386:Sequence Homology, Amino Acid; D014764:Viral Proteins / Q000737:chemistry* / Q000378:metabolism
D004268:DNA-Binding Proteins; D014764:Viral Proteins; D000255:Adenosine Triphosphate; D009713:Nucleotidyltransferases; D011088:DNA Ligases