2AU3
Crystal Structure of the Aquifex aeolicus primase (Zinc Binding and RNA Polymerase Domains)
Summary for 2AU3
| Entry DOI | 10.2210/pdb2au3/pdb |
| Descriptor | DNA primase, ZINC ION (3 entities in total) |
| Functional Keywords | zinc ribbon, toprim, rna polymerase, dna replication, transferase |
| Biological source | Aquifex aeolicus |
| Total number of polymer chains | 1 |
| Total formula weight | 46756.92 |
| Authors | Corn, J.E.,Pease, P.J.,Hura, G.L.,Berger, J.M. (deposition date: 2005-08-26, release date: 2005-11-15, Last modification date: 2024-04-03) |
| Primary citation | Corn, J.E.,Pease, P.J.,Hura, G.L.,Berger, J.M. Crosstalk between primase subunits can act to regulate primer synthesis in trans. Mol.Cell, 20:391-401, 2005 Cited by PubMed Abstract: The coordination of primase function within the replisome is an essential but poorly understood feature of lagging strand synthesis. By using crystallography and small-angle X-ray scattering (SAXS), we show that functional elements of bacterial primase transition between two dominant conformations: an extended form that uncouples a regulatory domain from its associated RNA polymerase core and a compact state that sequesters the regulatory region from the site of primer synthesis. FRET studies and priming assays reveal that the regulatory domain of one primase subunit productively associates with nucleic acid that is bound to the polymerase domain of a second protomer in trans. This intersubunit interaction allows primase to select initiation sites on template DNA and implicates the regulatory domain as a "molecular brake" that restricts primer length. Our data suggest that the replisome may cooperatively use multiple primases and this conformational switch to control initiation frequency, processivity, and ultimately, Okazaki fragment synthesis. PubMed: 16285921DOI: 10.1016/j.molcel.2005.09.004 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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