1EQN
E.COLI PRIMASE CATALYTIC CORE
Summary for 1EQN
| Entry DOI | 10.2210/pdb1eqn/pdb |
| Descriptor | DNA PRIMASE (1 entity in total) |
| Functional Keywords | toprim domain, rossmann fold, transferase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 5 |
| Total formula weight | 183104.70 |
| Authors | Podobnik, M.,McInerney, P.,O'Donnell, M.,Kuriyan, J. (deposition date: 2000-04-05, release date: 2000-06-30, Last modification date: 2024-11-06) |
| Primary citation | Podobnik, M.,McInerney, P.,O'Donnell, M.,Kuriyan, J. A TOPRIM domain in the crystal structure of the catalytic core of Escherichia coli primase confirms a structural link to DNA topoisomerases. J.Mol.Biol., 300:353-362, 2000 Cited by PubMed Abstract: Primases synthesize short RNA strands on single-stranded DNA templates, thereby generating the hybrid duplexes required for the initiation of synthesis by DNA polymerases. We present the crystal structure of the catalytic unit of a primase enzyme, that of a approximately 320 residue fragment of Escherichia coli primase, determined at 2.9 A resolution. Central to the catalytic unit is a TOPRIM domain that is strikingly similar in its structure to that of corresponding domains in DNA topoisomerases, but is unrelated to the catalytic centers of other DNA or RNA polymerases. The catalytic domain of primase is crescent-shaped, and the concave face of the crescent is predicted to accommodate about 10 base-pairs of RNA-DNA duplex in a loose interaction, thereby limiting processivity. PubMed: 10873470DOI: 10.1006/jmbi.2000.3844 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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