1A0I
ATP-DEPENDENT DNA LIGASE FROM BACTERIOPHAGE T7 COMPLEX WITH ATP
Summary for 1A0I
| Entry DOI | 10.2210/pdb1a0i/pdb |
| Descriptor | DNA LIGASE, ADENOSINE-5'-TRIPHOSPHATE (3 entities in total) |
| Functional Keywords | ligase, dna replication |
| Biological source | Enterobacteria phage T7 |
| Total number of polymer chains | 1 |
| Total formula weight | 40395.68 |
| Authors | Subramanya, H.S.,Doherty, A.J.,Ashford, S.R.,Wigley, D.B. (deposition date: 1997-12-01, release date: 1998-03-25, Last modification date: 2024-02-07) |
| Primary citation | Subramanya, H.S.,Doherty, A.J.,Ashford, S.R.,Wigley, D.B. Crystal structure of an ATP-dependent DNA ligase from bacteriophage T7. Cell(Cambridge,Mass.), 85:607-615, 1996 Cited by PubMed Abstract: 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. PubMed: 8653795DOI: 10.1016/S0092-8674(00)81260-X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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