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1tc3

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==TRANSPOSASE TC3A1-65 FROM CAENORHABDITIS ELEGANS==
==TRANSPOSASE TC3A1-65 FROM CAENORHABDITIS ELEGANS==
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<StructureSection load='1tc3' size='340' side='right' caption='[[1tc3]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
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<StructureSection load='1tc3' size='340' side='right'caption='[[1tc3]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1tc3]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Caeel Caeel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TC3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TC3 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1tc3]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TC3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TC3 FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TC3A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.45&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tc3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tc3 OCA], [http://pdbe.org/1tc3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tc3 RCSB], [http://www.ebi.ac.uk/pdbsum/1tc3 PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1tc3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tc3 OCA], [https://pdbe.org/1tc3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tc3 RCSB], [https://www.ebi.ac.uk/pdbsum/1tc3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tc3 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/TC3A_CAEEL 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.
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[https://www.uniprot.org/uniprot/TC3A_CAEEL 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.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The crystal structure of the complex between the N-terminal DNA-binding domain of Tc3 transposase and an oligomer of transposon DNA has been determined. The specific DNA-binding domain contains three alpha-helices, of which two form a helix-turn-helix (HTH) motif. The recognition of transposon DNA by the transposase is mediated through base-specific contacts and complementarity between protein and sequence-dependent deformations of the DNA. The HTH motif makes four base-specific contacts with the major groove, and the N-terminus makes three base-specific contacts with the minor groove. The DNA oligomer adopts a non-linear B-DNA conformation, made possible by a stretch of seven G:C base pairs at one end and a TATA sequence towards the other end. Extensive contacts (seven salt bridges and 16 hydrogen bonds) of the protein with the DNA backbone allow the protein to probe and recognize the sequence-dependent DNA deformation. The DNA-binding domain forms a dimer in the crystals. Each monomer binds a separate transposon end, implying that the dimer plays a role in synapsis, necessary for the simultaneous cleavage of both transposon termini.
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Crystal structure of the specific DNA-binding domain of Tc3 transposase of C.elegans in complex with transposon DNA.,van Pouderoyen G, Ketting RF, Perrakis A, Plasterk RH, Sixma TK EMBO J. 1997 Oct 1;16(19):6044-54. PMID:9312061<ref>PMID:9312061</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1tc3" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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*[[Transposase|Transposase]]
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*[[Transposase 3D structures|Transposase 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Caeel]]
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[[Category: Caenorhabditis elegans]]
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[[Category: Ketting, R F]]
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[[Category: Large Structures]]
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[[Category: Perrakis, A]]
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[[Category: Ketting RF]]
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[[Category: Plasterk, R H.A]]
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[[Category: Perrakis A]]
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[[Category: Pouderoyen, G Van]]
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[[Category: Plasterk RHA]]
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[[Category: Sixma, T K]]
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[[Category: Sixma TK]]
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[[Category: Dna binding]]
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[[Category: Van Pouderoyen G]]
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[[Category: Dna binding protein-dna complex]]
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[[Category: Helix-turn-helix]]
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[[Category: Tc1/mariner family]]
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[[Category: Transposase]]
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Current revision

TRANSPOSASE TC3A1-65 FROM CAENORHABDITIS ELEGANS

PDB ID 1tc3

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