1FVI
CRYSTAL STRUCTURE OF CHLORELLA VIRUS DNA LIGASE-ADENYLATE
Summary for 1FVI
| Entry DOI | 10.2210/pdb1fvi/pdb |
| Descriptor | CHLORELLA VIRUS DNA LIGASE-ADENYLATE, SULFATE ION, ADENOSINE MONOPHOSPHATE, ... (4 entities in total) |
| Functional Keywords | adenylated dna ligase, ligase |
| Biological source | Chlorella virus |
| Total number of polymer chains | 1 |
| Total formula weight | 34567.48 |
| Authors | Odell, M.,Sriskanda, V.,Shuman, S.,Nikolov, D.B. (deposition date: 2000-09-20, release date: 2000-11-22, Last modification date: 2024-11-20) |
| Primary citation | Odell, M.,Sriskanda, V.,Shuman, S.,Nikolov, D.B. Crystal structure of eukaryotic DNA ligase-adenylate illuminates the mechanism of nick sensing and strand joining. Mol.Cell, 6:1183-1193, 2000 Cited by PubMed Abstract: Chlorella virus DNA ligase is the smallest eukaryotic ATP-dependent ligase known; it has an intrinsic nick-sensing function and suffices for yeast cell growth. Here, we report the 2.0 A crystal structure of the covalent ligase-AMP reaction intermediate. The conformation of the adenosine nucleoside and contacts between the enzyme and the ribose sugar have undergone a significant change compared to complexes of T7 ligase with ATP or mRNA capping enzyme with GTP. The conformational switch allows the 3' OH of AMP to coordinate directly the 5' PO(4) of the nick. The structure explains why nick sensing is restricted to adenylated ligase and why the 5' phosphate is required for DNA binding. We identify a metal binding site on ligase-adenylate and propose a mechanism of nick recognition and catalysis supported by mutational data. PubMed: 11106756DOI: 10.1016/S1097-2765(00)00115-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
Download full validation report
