1B04
STRUCTURE OF THE ADENYLATION DOMAIN OF AN NAD+ DEPENDENT LIGASE
Summary for 1B04
| Entry DOI | 10.2210/pdb1b04/pdb |
| Descriptor | PROTEIN (DNA LIGASE) (2 entities in total) |
| Functional Keywords | ligase, dna replication |
| Biological source | Geobacillus stearothermophilus |
| Total number of polymer chains | 2 |
| Total formula weight | 71664.70 |
| Authors | Singleton, M.R.,Hakansson, K.,Timson, D.J.,Wigley, D.B. (deposition date: 1998-11-16, release date: 1999-11-22, Last modification date: 2024-02-07) |
| Primary citation | Singleton, M.R.,Hakansson, K.,Timson, D.J.,Wigley, D.B. Structure of the adenylation domain of an NAD+-dependent DNA ligase. Structure Fold.Des., 7:35-42, 1999 Cited by PubMed Abstract: DNA ligases catalyse phosphodiester bond formation between adjacent bases in nicked DNA, thereby sealing the nick. A key step in the catalytic mechanism is the formation of an adenylated DNA intermediate. The adenyl group is derived from either ATP (in eucaryotes and archaea) or NAD+4 (in bacteria). This difference in cofactor specificity suggests that DNA ligase may be a useful antibiotic target. PubMed: 10368271DOI: 10.1016/S0969-2126(99)80007-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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