8edg

Cryo-EM structure of the Hermes transposase bound to two left-ends of its DNA transposon

spinqualitylabelsall models 8edg, resolution 4.64Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8edg is a 12 chain structure with sequence from Musca domestica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 4.64Å Ligands: ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q25438_MUSDO Publication Abstract from PubMed The Hermes DNA transposon is a member of the eukaryotic hAT superfamily, and its transposase forms a ring-shaped tetramer of dimers. Our investigation, combining biochemical, crystallography and cryo-electron microscopy, and in-cell assays, shows that the full-length Hermes octamer extensively interacts with its transposon left-end through multiple BED domains of three Hermes protomers contributed by three dimers explaining the role of the unusual higher-order assembly. By contrast, the right-end is bound to no BED domains at all. Thus, this work supports a model in which Hermes multimerizes to gather enough BED domains to find its left-end among the abundant genomic DNA, facilitating the subsequent interaction with the right-end. Zinc-finger BED domains drive the formation of the active Hermes transpososome by asymmetric DNA binding.,Lannes L, Furman CM, Hickman AB, Dyda F Nat Commun. 2023 Jul 25;14(1):4470. doi: 10.1038/s41467-023-40210-3. PMID:37491363 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Transposase 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA