1u78
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(New page: 200px<br /><applet load="1u78" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u78, resolution 2.69Å" /> '''Structure of the bip...)
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Revision as of 01:46, 21 November 2007
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Structure of the bipartite DNA-binding domain of Tc3 transposase bound to transposon DNA
Overview
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.
About this Structure
1U78 is a Single protein structure of sequence from Caenorhabditis elegans. Full crystallographic information is available from OCA.
Reference
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
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