|
|
| Line 3: |
Line 3: |
| | <StructureSection load='6dgb' size='340' side='right'caption='[[6dgb]], [[Resolution|resolution]] 2.52Å' scene=''> | | <StructureSection load='6dgb' size='340' side='right'caption='[[6dgb]], [[Resolution|resolution]] 2.52Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6dgb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DGB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DGB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6dgb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DGB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6DGB FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IS1535 TnpA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</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]] 2.52Å</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=6dgb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dgb OCA], [http://pdbe.org/6dgb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dgb RCSB], [http://www.ebi.ac.uk/pdbsum/6dgb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dgb 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=6dgb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dgb OCA], [https://pdbe.org/6dgb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6dgb RCSB], [https://www.ebi.ac.uk/pdbsum/6dgb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6dgb ProSAT]</span></td></tr> |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/I6WZS4_MYCTU I6WZS4_MYCTU] |
| - | 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>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 6dgb" style="background-color:#fffaf0;"></div>
| + | |
| - | == References ==
| + | |
| - | <references/>
| + | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Cascio, D]] | + | [[Category: Mycobacterium tuberculosis]] |
| - | [[Category: Chen, W Y]] | + | [[Category: Cascio D]] |
| - | [[Category: Hancock, S P]] | + | [[Category: Chen WY]] |
| - | [[Category: Johnson, R C]] | + | [[Category: Hancock SP]] |
| - | [[Category: 607-like serine recombinase]] | + | [[Category: Johnson RC]] |
| - | [[Category: Hydrolase]]
| + | |
