Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4DM0

TN5 transposase: 20MER OUTSIDE END 2 MN complex

Replaces:  1MURReplaces:  1L1A
Summary for 4DM0
Entry DOI10.2210/pdb4dm0/pdb
Related1MUH 1MUS
DescriptorTransposase for transposon Tn5, DNA TRANSFERRED STRAND, DNA NON-TRANSFERRED STRAND, ... (6 entities in total)
Functional Keywordstransposase, ribonuclease h-like motif, protein-dna complex, synaptic complex, dna recombination-dna complex, hydrolase-dna complex, hydrolase/dna
Biological sourceEscherichia coli
More
Total number of polymer chains3
Total formula weight66173.18
Authors
Klenchin, V.A.,Lovell, S.,Goryshin, I.Y.,Reznikoff, W.R.,Rayment, I. (deposition date: 2012-02-06, release date: 2012-02-22, Last modification date: 2023-09-13)
Primary citationLovell, S.,Goryshin, I.Y.,Reznikoff, W.R.,Rayment, I.
Two-metal active site binding of a TN5 transposase synaptic complex
Nat.Struct.Biol., 9:278-281, 2002
Cited by
PubMed Abstract: A synaptic complex of Tn5 transposase with an extended outside end DNA duplex was prepared and crystallized, and its crystal structure was determined in an effort to reveal the role of metal ions in catalysis. Two Mn2+ ions bound to the active site when a single nucleotide of donor DNA was added to the 3' end of the transferred strand. Marked conformational changes were observed in the DNA bases closest to the active site. The position of the metal ions and the conformational changes of the DNA provide insight into the mechanism of hairpin formation and cleavage, and is consistent with a two-metal model for catalysis.
PubMed: 11896402
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

246704

PDB entries from 2025-12-24

PDB statisticsPDBj update infoContact PDBjnumon