6is8
Crystal structure of ZmMoc1 D115N mutant in complex with Holliday junctionCrystal structure of ZmMoc1 D115N mutant in complex with Holliday junction
Structural highlights
FunctionPublication Abstract from PubMedThe Holliday junction (HJ) is a key intermediate during homologous recombination and DNA double-strand break repair. Timely HJ resolution by resolvases is critical for maintaining genome stability. The mechanisms underlying sequence-specific substrate recognition and cleavage by resolvases remain elusive. The monokaryotic chloroplast 1 protein (MOC1) specifically cleaves four-way DNA junctions in a sequence-specific manner. Here, we report the crystal structures of MOC1 from Zea mays, alone or bound to HJ DNA. MOC1 uses a unique beta-hairpin to embrace the DNA junction. A base-recognition motif specifically interacts with the junction center, inducing base flipping and pseudobase-pair formation at the strand-exchanging points. Structures of MOC1 bound to HJ and different metal ions support a two-metal ion catalysis mechanism. Further molecular dynamics simulations and biochemical analyses reveal a communication between specific substrate recognition and metal ion-dependent catalysis. Our study thus provides a mechanism for how a resolvase turns substrate specificity into catalytic efficiency. Structural basis of sequence-specific Holliday junction cleavage by MOC1.,Lin H, Zhang D, Zuo K, Yuan C, Li J, Huang M, Lin Z Nat Chem Biol. 2019 Oct 14. pii: 10.1038/s41589-019-0377-4. doi:, 10.1038/s41589-019-0377-4. PMID:31611704[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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