1U78

Structure of the bipartite DNA-binding domain of Tc3 transposase bound to transposon DNA

Summary for 1U78

• Entry DOI: 10.2210/pdb1u78/pdb
• Related: 1TC3
• Descriptor: 26-MER, transposable element tc3 transposase, ... (4 entities in total)
• Functional Keywords: transposase, transposon dna, bipartite dna-binding, hth-motif, dna binding protein-dna complex, dna binding protein/dna
• Biological source: Caenorhabditis elegans
• Cellular location: Nucleus: P34257
• Total number of polymer chains: 3
• Total formula weight: 32187.24

Authors

Watkins, S.,van Pouderoyen, G.,Sixma, T.K. (deposition date: 2004-08-03, release date: 2004-08-31, Last modification date: 2023-10-25)

Primary citation

Watkins, S.,van Pouderoyen, G.,Sixma, T.K.
Structural analysis of the bipartite DNA-binding domain of Tc3 transposase bound to transposon DNA
Nucleic Acids Res., 32:4306-4312, 2004

PubMed Abstract: The bipartite DNA-binding domain of Tc3 transposase, Tc3A, was crystallized in complex with its transposon recognition sequence. In the structure the two DNA-binding domains form structurally related helix-turn-helix (HTH) motifs. They both bind to the major groove on a single DNA oligomer, separated by a linker that interacts closely with the minor groove. The structure resembles that of the transcription factor Pax6 DNA-binding domain, but the relative orientation of the HTH-domain is different. The DNA conformation is distorted, characterized by local narrowing of the minor groove and bends at both ends. The protein-DNA recognition takes place through base and backbone contacts, as well as shape-recognition of the distortions in the DNA. Charged interactions are primarily found in the N-terminal domain and the linker indicating that these may form the initial contact area. Two independent dimer interfaces could be relevant for bringing together transposon ends and for binding to a direct repeat site in the transposon end. In contrast to the Tn5 synaptic complex, the two Tc3A DNA-binding domains bind to a single Tc3 transposon end.

PubMed: 15304566
DOI: 10.1093/nar/gkh770

Experimental method

X-RAY DIFFRACTION (2.69 Å)