1a0i
ATP-DEPENDENT DNA LIGASE FROM BACTERIOPHAGE T7 COMPLEX WITH ATP
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| , resolution 2.6Å | |||||||
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| Ligands: | |||||||
| Gene: | LIG (Enterobacteria phage T7) | ||||||
| Activity: | DNA ligase (ATP), with EC number 6.5.1.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
OverviewOverview
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.
About this StructureAbout this Structure
1A0I is a Single protein structure of sequence from Enterobacteria phage t7. The following page contains interesting information on the relation of 1A0I with [DNA Ligase]. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of an ATP-dependent DNA ligase from bacteriophage T7., Subramanya HS, Doherty AJ, Ashford SR, Wigley DB, Cell. 1996 May 17;85(4):607-15. PMID:8653795
Page seeded by OCA on Sun Mar 30 18:30:32 2008