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| ==Structure of the Tn1549 transposon Integrase (aa 82-397, Y379F) in complex with transposon right end DNA== | | ==Structure of the Tn1549 transposon Integrase (aa 82-397, Y379F) in complex with transposon right end DNA== |
- | <StructureSection load='6emy' size='340' side='right' caption='[[6emy]], [[Resolution|resolution]] 2.50Å' scene=''> | + | <StructureSection load='6emy' size='340' side='right'caption='[[6emy]], [[Resolution|resolution]] 2.50Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[6emy]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/"enterococcus_proteiformis"_thiercelin_and_jouhaud_1903 "enterococcus proteiformis" thiercelin and jouhaud 1903]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EMY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EMY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6emy]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridioides_difficile Clostridioides difficile] and [https://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EMY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6EMY FirstGlance]. <br> |
- | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">int ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1351 "Enterococcus proteiformis" Thiercelin and Jouhaud 1903])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> |
- | <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=6emy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6emy OCA], [http://pdbe.org/6emy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6emy RCSB], [http://www.ebi.ac.uk/pdbsum/6emy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6emy ProSAT]</span></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=6emy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6emy OCA], [https://pdbe.org/6emy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6emy RCSB], [https://www.ebi.ac.uk/pdbsum/6emy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6emy ProSAT]</span></td></tr> |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/Q7BP35_ENTFL Q7BP35_ENTFL] |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| ==See Also== | | ==See Also== |
- | *[[Retroviral Integrase|Retroviral Integrase]] | + | *[[Retroviral integrase 3D structures|Retroviral integrase 3D structures]] |
| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Enterococcus proteiformis thiercelin and jouhaud 1903]] | + | [[Category: Clostridioides difficile]] |
- | [[Category: Barabas, O]] | + | [[Category: Enterococcus faecalis]] |
- | [[Category: Rubio-Cosials, A]] | + | [[Category: Large Structures]] |
- | [[Category: Schulz, E C]] | + | [[Category: Barabas O]] |
- | [[Category: Antibiotic resistance transfer]] | + | [[Category: Rubio-Cosials A]] |
- | [[Category: Recombination]]
| + | [[Category: Schulz EC]] |
- | [[Category: Tn916-like conjugative transposon]]
| + | |
- | [[Category: Transposase protein-dna complex]] | + | |
- | [[Category: Tyrosine recombinase]]
| + | |
- | [[Category: Y-transposase]]
| + | |
| Structural highlights
Function
Q7BP35_ENTFL
Publication Abstract from PubMed
Conjugative transposition drives the emergence of multidrug resistance in diverse bacterial pathogens, yet the mechanisms are poorly characterized. The Tn1549 conjugative transposon propagates resistance to the antibiotic vancomycin used for severe drug-resistant infections. Here, we present four high-resolution structures of the conserved Y-transposase of Tn1549 complexed with circular transposon DNA intermediates. The structures reveal individual transposition steps and explain how specific DNA distortion and cleavage mechanisms enable DNA strand exchange with an absolute minimum homology requirement. This appears to uniquely allow Tn916-like conjugative transposons to bypass DNA homology and insert into diverse genomic sites, expanding gene transfer. We further uncover a structural regulatory mechanism that prevents premature cleavage of the transposon DNA before a suitable target DNA is found and generate a peptide antagonist that interferes with the transposase-DNA structure to block transposition. Our results reveal mechanistic principles of conjugative transposition that could help control the spread of antibiotic resistance genes.
Transposase-DNA Complex Structures Reveal Mechanisms for Conjugative Transposition of Antibiotic Resistance.,Rubio-Cosials A, Schulz EC, Lambertsen L, Smyshlyaev G, Rojas-Cordova C, Forslund K, Karaca E, Bebel A, Bork P, Barabas O Cell. 2018 Mar 22;173(1):208-220.e20. doi: 10.1016/j.cell.2018.02.032. Epub 2018 , Mar 15. PMID:29551265[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Rubio-Cosials A, Schulz EC, Lambertsen L, Smyshlyaev G, Rojas-Cordova C, Forslund K, Karaca E, Bebel A, Bork P, Barabas O. Transposase-DNA Complex Structures Reveal Mechanisms for Conjugative Transposition of Antibiotic Resistance. Cell. 2018 Mar 22;173(1):208-220.e20. doi: 10.1016/j.cell.2018.02.032. Epub 2018 , Mar 15. PMID:29551265 doi:http://dx.doi.org/10.1016/j.cell.2018.02.032
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