6dgc: Difference between revisions
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==Crystal structure of the C-terminal catalytic domain of ISC1926 TnpA, an IS607-like serine recombinase== | |||
<StructureSection load='6dgc' size='340' side='right'caption='[[6dgc]], [[Resolution|resolution]] 2.92Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6dgc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfolobus_sp._L00_11 Sulfolobus sp. L00 11]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DGC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6DGC FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.92Å</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6dgc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dgc OCA], [https://pdbe.org/6dgc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6dgc RCSB], [https://www.ebi.ac.uk/pdbsum/6dgc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6dgc ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q5MPE7_9CREN Q5MPE7_9CREN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
IS607-family transposons are unusual because they do not have terminal inverted repeats or generate target site duplications. They encode two protein-coding genes, but only tnpA is required for transposition. Our X-ray structures confirm that TnpA is a member of the serine recombinase (SR) family, but the chemically-inactive quaternary structure of the dimer, along with the N-terminal location of the DNA binding domain, are different from other SRs. TnpA dimers from IS1535 cooperatively associate with multiple subterminal repeats, which together with additional nonspecific binding, form a nucleoprotein filament on one transposon end that efficiently captures a second unbound end to generate the paired-end complex (PEC). Formation of the PEC does not require a change in the dimeric structure of the catalytic domain, but remodeling of the C-terminal alpha-helical region is involved. We posit that the PEC recruits a chemically-active conformer of TnpA to the transposon end to initiate DNA chemistry. | |||
Multiple serine transposase dimers assemble the transposon-end synaptic complex during IS607-family transposition.,Chen W, Mandali S, Hancock SP, Kumar P, Collazo M, Cascio D, Johnson RC Elife. 2018 Oct 5;7. pii: 39611. doi: 10.7554/eLife.39611. PMID:30289389<ref>PMID:30289389</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6dgc" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: Johnson | ==See Also== | ||
[[Category: | *[[Transposase 3D structures|Transposase 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Sulfolobus sp. L00 11]] | |||
[[Category: Cascio D]] | |||
[[Category: Hancock SP]] | |||
[[Category: Johnson RC]] | |||
[[Category: Kumar P]] | |||
Latest revision as of 09:05, 11 October 2023
Crystal structure of the C-terminal catalytic domain of ISC1926 TnpA, an IS607-like serine recombinaseCrystal structure of the C-terminal catalytic domain of ISC1926 TnpA, an IS607-like serine recombinase
Structural highlights
FunctionPublication Abstract from PubMedIS607-family transposons are unusual because they do not have terminal inverted repeats or generate target site duplications. They encode two protein-coding genes, but only tnpA is required for transposition. Our X-ray structures confirm that TnpA is a member of the serine recombinase (SR) family, but the chemically-inactive quaternary structure of the dimer, along with the N-terminal location of the DNA binding domain, are different from other SRs. TnpA dimers from IS1535 cooperatively associate with multiple subterminal repeats, which together with additional nonspecific binding, form a nucleoprotein filament on one transposon end that efficiently captures a second unbound end to generate the paired-end complex (PEC). Formation of the PEC does not require a change in the dimeric structure of the catalytic domain, but remodeling of the C-terminal alpha-helical region is involved. We posit that the PEC recruits a chemically-active conformer of TnpA to the transposon end to initiate DNA chemistry. Multiple serine transposase dimers assemble the transposon-end synaptic complex during IS607-family transposition.,Chen W, Mandali S, Hancock SP, Kumar P, Collazo M, Cascio D, Johnson RC Elife. 2018 Oct 5;7. pii: 39611. doi: 10.7554/eLife.39611. PMID:30289389[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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