9B0L
Cryo-EM structure of Acanthamoeba polyphaga mimivirus Fanzor2 ternary complex
Summary for 9B0L
Entry DOI | 10.2210/pdb9b0l/pdb |
EMDB information | 44046 |
Descriptor | DNA (5'-D(P*GP*AP*CP*GP*GP*TP*CP*GP*GP*GP*C)-3'), TnpB-like protein L79, DNA (5'-D(P*CP*CP*CP*A)-3'), ... (7 entities in total) |
Functional Keywords | transposon, fanzor, cryo-em, dna binding protein-dna-rna complex, dna binding protein/dna/rna |
Biological source | Acanthamoeba polyphaga mimivirus More |
Total number of polymer chains | 5 |
Total formula weight | 151627.47 |
Authors | Qayyum, M.Z.,Schargel, R.D.,Tanwar, A.S.,Kellogg, E.H.,Kalathur, R.C. (deposition date: 2024-03-12, release date: 2024-10-09) |
Primary citation | Schargel, R.D.,Qayyum, M.Z.,Tanwar, A.S.,Kalathur, R.C.,Kellogg, E.H. Structure of Fanzor2 reveals insights into the evolution of the TnpB superfamily. Nat.Struct.Mol.Biol., 2024 Cited by PubMed Abstract: RNA-guided endonucleases, once thought to be exclusive to prokaryotes, have been recently identified in eukaryotes and are called Fanzors. They are classified into two clades, Fanzor1 and Fanzor2. Here we present the cryo-electron microscopy structure of Acanthamoeba polyphaga mimivirus Fanzor2, revealing its ωRNA architecture, active site and features involved in transposon-adjacent motif recognition. A comparison to Fanzor1 and TnpB structures highlights divergent evolutionary paths, advancing our understanding of RNA-guided endonucleases. PubMed: 39354233DOI: 10.1038/s41594-024-01394-4 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (2.99 Å) |
Structure validation
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