6P7B
Crystal structure of Fowlpox virus resolvase and substrate Holliday junction DNA complex
Summary for 6P7B
| Entry DOI | 10.2210/pdb6p7b/pdb |
| Descriptor | Holliday junction resolvase, DNA (29-MER) (3 entities in total) |
| Functional Keywords | resolvase-dna complex, hydrolase-dna complex, transcription, hydrolase/dna |
| Biological source | Fowlpox virus (FPV) More |
| Total number of polymer chains | 6 |
| Total formula weight | 87293.00 |
| Authors | Li, N.,Shi, K.,Rao, T.,Banerjee, S.,Aihara, H. (deposition date: 2019-06-05, release date: 2020-04-29, Last modification date: 2024-03-13) |
| Primary citation | Li, N.,Shi, K.,Rao, T.,Banerjee, S.,Aihara, H. Structural insights into the promiscuous DNA binding and broad substrate selectivity of fowlpox virus resolvase. Sci Rep, 10:393-393, 2020 Cited by PubMed Abstract: Fowlpox virus resolvase (Fpr) is an endonuclease that cleaves a broad range of branched DNA structures, including the Holliday junction (HJ), with little sequence-specificity. To better understand the mechanisms underlying its relaxed substrate specificity, we determined the crystal structures of Fpr and that in a novel complex with HJ at 3.1-Å resolution. In the Fpr-HJ complex, two Fpr dimers use several distinct regions to interact with different DNA structural motifs, showing versatility in DNA-binding. Biochemical and solution NMR data support the existence of non-canonical modes of HJ interaction in solution. The binding of Fpr to various DNA motifs are mediated by its flat DNA-binding surface, which is centered on a short loop spanning K61 to I72 and flanked by longer α-helices at the outer edges, and basic side grooves near the dimer interface. Replacing the Fpr loop K61~I72 with a longer loop from Thermus thermophilus RuvC (E71~A87) endows Fpr with an enhanced selectivity toward HJ cleavage but with a target sequence preference distinct from that of RuvC, highlighting a unique role of this loop region in Fpr-HJ interaction. Our work helps explain the broad substrate selectivity of Fpr and suggests a possible mode of its association with poxvirus hairpin telomeres. PubMed: 31941902DOI: 10.1038/s41598-019-56825-w PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.317 Å) |
Structure validation
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