1u78

From Proteopedia

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

Structural highlights

1u78 is a 3 chain structure with sequence from Caenorhabditis elegans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.69Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TC3A_CAEEL Binds specifically to the terminal nucleotides of the TC3 inverted repeat. Its expression results in frequent excision and transposition of endogenous TC3 elements. TC3 transposase acts by making double strand breaks at the ends of TC3 element. The excised element would then be inserted into a target sequence.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

Structural analysis of the bipartite DNA-binding domain of Tc3 transposase bound to transposon DNA.,Watkins S, van Pouderoyen G, Sixma TK Nucleic Acids Res. 2004 Aug 10;32(14):4306-12. Print 2004. PMID:15304566^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Watkins S, van Pouderoyen G, Sixma TK. Structural analysis of the bipartite DNA-binding domain of Tc3 transposase bound to transposon DNA. Nucleic Acids Res. 2004 Aug 10;32(14):4306-12. Print 2004. PMID:15304566 doi:10.1093/nar/gkh770