9y66

attLsym bound serine integrase complex in the dimeric state

spinqualitylabelsall models 9y66, resolution 3.31Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9y66 is a 4 chain structure with sequence from Bacillus virus SPbeta. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.31Å Ligands: ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Large serine integrases (LSIs) catalyze unidirectional site-specific DNA recombination reactions, yet those reactions are reversed by the presence of a cognate recombination directionality factor (RDF). Mechanistic understanding of directionality control has been hampered by a lack of structural information. Here, we use cryo-electron microscopy (cryo-EM) to determine the structures of six SPbeta integrase-DNA complexes along the integrative (-RDF) and excisive (+RDF) reaction pathways, at 4.16-7.18A resolution. Our findings reveal how RDF-mediated repositioning of an integrase subdomain (1) dictates which pairs of DNA sites can be assembled into a synaptic complex to initiate recombination and (2) dictates which product complexes will be conformationally locked, preventing the back reaction. These mechanistic insights provide a conceptual framework for engineering efficient and versatile genome editing tools. Structural basis of directionality control in large serine integrases.,Shin H, Pigli Y, Reyes TP, Fuller JR, Olorunniji FJ, Rice PA bioRxiv [Preprint]. 2025 Jan 13:2025.01.03.631226. doi: , 10.1101/2025.01.03.631226. PMID:39803483 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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