6ZP9
Cyanophage S-2L Primase-Polymerase (PrimPol), AEP domain (PP-N190)
Summary for 6ZP9
| Entry DOI | 10.2210/pdb6zp9/pdb |
| Descriptor | PrimPol AEP domain (PP-N190), CALCIUM ION (3 entities in total) |
| Functional Keywords | s-2l, aep, primpol, ppl1, viral protein |
| Biological source | Cyanophage S-2L |
| Total number of polymer chains | 2 |
| Total formula weight | 43206.44 |
| Authors | Czernecki, D.,Legrand, P.,Delarue, M. (deposition date: 2020-07-08, release date: 2021-03-03, Last modification date: 2024-05-15) |
| Primary citation | Czernecki, D.,Legrand, P.,Tekpinar, M.,Rosario, S.,Kaminski, P.A.,Delarue, M. How cyanophage S-2L rejects adenine and incorporates 2-aminoadenine to saturate hydrogen bonding in its DNA. Nat Commun, 12:2420-2420, 2021 Cited by PubMed Abstract: Bacteriophages have long been known to use modified bases in their DNA to prevent cleavage by the host's restriction endonucleases. Among them, cyanophage S-2L is unique because its genome has all its adenines (A) systematically replaced by 2-aminoadenines (Z). Here, we identify a member of the PrimPol family as the sole possible polymerase of S-2L and we find it can incorporate both A and Z in front of a T. Its crystal structure at 1.5 Å resolution confirms that there is no structural element in the active site that could lead to the rejection of A in front of T. To resolve this contradiction, we show that a nearby gene is a triphosphohydolase specific of dATP (DatZ), that leaves intact all other dNTPs, including dZTP. This explains the absence of A in S-2L genome. Crystal structures of DatZ with various ligands, including one at sub-angstrom resolution, allow to describe its mechanism as a typical two-metal-ion mechanism and to set the stage for its engineering. PubMed: 33893297DOI: 10.1038/s41467-021-22626-x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.50002224932 Å) |
Structure validation
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