6P7B

Crystal structure of Fowlpox virus resolvase and substrate Holliday junction DNA complex

6P7B の概要

• エントリーDOI: 10.2210/pdb6p7b/pdb
• 分子名称: Holliday junction resolvase, DNA (29-MER) (3 entities in total)
• 機能のキーワード: resolvase-dna complex, hydrolase-dna complex, transcription, hydrolase/dna
• 由来する生物種: Fowlpox virus (FPV); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 87293.00

構造登録者

Li, N.,Shi, K.,Rao, T.,Banerjee, S.,Aihara, H. (登録日: 2019-06-05, 公開日: 2020-04-29, 最終更新日: 2024-03-13)

主引用文献

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

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: 31941902
DOI: 10.1038/s41598-019-56825-w

実験手法

X-RAY DIFFRACTION (3.317 Å)