Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structures of a RAG-like transposase during cut-and-paste transposition.
Journal, issue, pages	Nature, Vol. 575, Issue 7783, Page 540-544, Year 2019
Publish date	Nov 13, 2019
Authors	Chang Liu / Yang Yang / David G Schatz /
PubMed Abstract	Transposons have had a pivotal role in genome evolution and are believed to be the evolutionary progenitors of the RAG1-RAG2 recombinase, an essential component of the adaptive immune system in jawed ...Transposons have had a pivotal role in genome evolution and are believed to be the evolutionary progenitors of the RAG1-RAG2 recombinase, an essential component of the adaptive immune system in jawed vertebrates. Here we report one crystal structure and five cryo-electron microscopy structures of Transib, a RAG1-like transposase from Helicoverpa zea, that capture the entire transposition process from the apo enzyme to the terminal strand transfer complex with transposon ends covalently joined to target DNA, at resolutions of 3.0-4.6 Å. These structures reveal a butterfly-shaped complex that undergoes two cycles of marked conformational changes in which the 'wings' of the transposase unfurl to bind substrate DNA, close to execute cleavage, open to release the flanking DNA and close again to capture and attack target DNA. Transib possesses unique structural elements that compensate for the absence of a RAG2 partner, including a loop that interacts with the transposition target site and an accordion-like C-terminal tail that elongates and contracts to help to control the opening and closing of the enzyme and assembly of the active site. Our findings reveal the detailed reaction pathway of a eukaryotic cut-and-paste transposase and illuminate some of the earliest steps in the evolution of the RAG recombinase.
External links	Nature / PubMed:31723264 / PubMed Central
Methods	EM (single particle) / X-ray diffraction
Resolution	3.01 - 4.6 Å
Structure data	20452 6pqr EMDB-20452, PDB-6pqr: Cryo-EM structure of HzTransib/intact TIR substrate DNA pre-reaction complex (PRC) Method: EM (single particle) / Resolution: 3.4 Å 20453 6pqu EMDB-20453, PDB-6pqu: Cryo-EM structure of HzTransib/nicked TIR substrate DNA pre-reaction complex (PRC) Method: EM (single particle) / Resolution: 3.3 Å 20455 6pqx EMDB-20455, PDB-6pqx: Cryo-EM structure of HzTransib/nicked TIR substrate DNA hairpin forming complex (HFC) Method: EM (single particle) / Resolution: 4.6 Å 20456 6pqy EMDB-20456, PDB-6pqy: Cryo-EM structure of HzTransib/TIR DNA transposon end complex (TEC) Method: EM (single particle) / Resolution: 4.2 Å 20457 6pr5 EMDB-20457, PDB-6pr5: Cryo-EM structure of HzTransib strand transfer complex (STC) Method: EM (single particle) / Resolution: 3.3 Å PDB-6pqn: Crystal structure of HzTransib transposase Method: X-RAY DIFFRACTION / Resolution: 3.01 Å
Chemicals	ChemComp-ZN: Unknown entry ChemComp-PO4: PHOSPHATE ION ChemComp-GOL: GLYCEROL ChemComp-NA: Unknown entry ChemComp-HOH: WATER ChemComp-MG: Unknown entry ChemComp-K: Unknown entry ChemComp-CA: Unknown entry
Source	helicoverpa zea (corn earworm)
Keywords	RECOMBINATION / RAG-like transposase / DDE family enzyme / Transib / Evolution of RAG / recombination/dna / Terminal inverted repeat. / recombination-dna complex / Strand transfer.