1u78
From Proteopedia
(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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| - | [[Image:1u78.gif|left|200px]]<br /><applet load="1u78" size=" | + | [[Image:1u78.gif|left|200px]]<br /><applet load="1u78" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1u78, resolution 2.69Å" /> | caption="1u78, resolution 2.69Å" /> | ||
'''Structure of the bipartite DNA-binding domain of Tc3 transposase bound to transposon DNA'''<br /> | '''Structure of the bipartite DNA-binding domain of Tc3 transposase bound to transposon DNA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The bipartite DNA-binding domain of Tc3 transposase, Tc3A, was | + | 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== | ==About this Structure== | ||
| - | 1U78 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http:// | + | 1U78 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U78 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Caenorhabditis elegans]] | [[Category: Caenorhabditis elegans]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Pouderoyen, G | + | [[Category: Pouderoyen, G van.]] |
| - | [[Category: Sixma, T | + | [[Category: Sixma, T K.]] |
[[Category: Watkins, S.]] | [[Category: Watkins, S.]] | ||
[[Category: bipartite dna-binding]] | [[Category: bipartite dna-binding]] | ||
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[[Category: transposon dna]] | [[Category: transposon dna]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:21:19 2008'' |
Revision as of 13:21, 21 February 2008
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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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