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| | <StructureSection load='6zns' size='340' side='right'caption='[[6zns]], [[Resolution|resolution]] 3.32Å' scene=''> | | <StructureSection load='6zns' size='340' side='right'caption='[[6zns]], [[Resolution|resolution]] 3.32Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6zns]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacsu Bacsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZNS OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6ZNS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6zns]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZNS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZNS FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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]] 3.32Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[6znp|6znp]], [[6znq|6znq]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">yprA, BSU22220 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</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=6zns FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zns OCA], [https://pdbe.org/6zns PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zns RCSB], [https://www.ebi.ac.uk/pdbsum/6zns PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zns ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6zns FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zns OCA], [http://pdbe.org/6zns PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6zns RCSB], [http://www.ebi.ac.uk/pdbsum/6zns PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6zns ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/YPRA_BACSU YPRA_BACSU] |
| - | Mitomycin repair factor A represents a family of DNA helicases that harbor a domain of unknown function (DUF1998) and support repair of mitomycin C-induced DNA damage by presently unknown molecular mechanisms. We determined crystal structures of Bacillus subtilis Mitomycin repair factor A alone and in complex with an ATP analog and/or DNA and conducted structure-informed functional analyses. Our results reveal a unique set of auxiliary domains appended to a dual-RecA domain core. Upon DNA binding, a Zn2+-binding domain, encompassing the domain of unknown function, acts like a drum that rolls out a canopy of helicase-associated domains, entrapping the substrate and tautening an inter-domain linker across the loading strand. Quantification of DNA binding, stimulated ATPase and helicase activities in the wild type and mutant enzyme variants in conjunction with the mode of coordination of the ATP analog suggest that Mitomycin repair factor A employs similar ATPase-driven conformational changes to translocate on DNA, with the linker ratcheting through the nucleotides like a 'skipping rope'. The electrostatic surface topology outlines a likely path for the displaced DNA strand. Our results reveal unique molecular mechanisms in a widespread family of DNA repair helicases linked to bacterial antibiotics resistance.
| + | |
| - | | + | |
| - | A skipping rope translocation mechanism in a widespread family of DNA repair helicases.,Roske JJ, Liu S, Loll B, Neu U, Wahl MC Nucleic Acids Res. 2020 Dec 9. pii: 6029183. doi: 10.1093/nar/gkaa1174. PMID:33300032<ref>PMID:33300032</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 6zns" style="background-color:#fffaf0;"></div>
| + | |
| - | == References ==
| + | |
| - | <references/>
| + | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacsu]] | + | [[Category: Bacillus subtilis subsp. subtilis str. 168]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Liu, S]] | + | [[Category: Liu S]] |
| - | [[Category: Loll, B]] | + | [[Category: Loll B]] |
| - | [[Category: Neu, U]] | + | [[Category: Neu U]] |
| - | [[Category: Roske, J J]] | + | [[Category: Roske JJ]] |
| - | [[Category: Wahl, M C]] | + | [[Category: Wahl MC]] |
| - | [[Category: Dna]]
| + | |
| - | [[Category: Duf1998]]
| + | |
| - | [[Category: Helicase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Mrfa]]
| + | |
| - | [[Category: Repair]]
| + | |
| - | [[Category: Ypra]]
| + | |
