|
|
| Line 3: |
Line 3: |
| | <StructureSection load='6vsx' size='340' side='right'caption='[[6vsx]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='6vsx' size='340' side='right'caption='[[6vsx]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6vsx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VSX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6VSX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6vsx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VSX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VSX FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">B4417_3167 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_helicase DNA helicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.12 3.6.4.12] </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=6vsx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vsx OCA], [https://pdbe.org/6vsx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vsx RCSB], [https://www.ebi.ac.uk/pdbsum/6vsx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vsx 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=6vsx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vsx OCA], [http://pdbe.org/6vsx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6vsx RCSB], [http://www.ebi.ac.uk/pdbsum/6vsx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6vsx ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/HELD_BACSU HELD_BACSU] Catalyzes the unwinding of duplex DNA in the 3' to 5' direction; this reaction is dependent on the hydrolysis of ATP.<ref>PMID:11544244</ref> |
| - | RNA synthesis is central to life, and RNA polymerase (RNAP) depends on accessory factors for recovery from stalled states and adaptation to environmental changes. Here, we investigated the mechanism by which a helicase-like factor HelD recycles RNAP. We report a cryo-EM structure of a complex between the Mycobacterium smegmatis RNAP and HelD. The crescent-shaped HelD simultaneously penetrates deep into two RNAP channels that are responsible for nucleic acids binding and substrate delivery to the active site, thereby locking RNAP in an inactive state. We show that HelD prevents non-specific interactions between RNAP and DNA and dissociates stalled transcription elongation complexes. The liberated RNAP can either stay dormant, sequestered by HelD, or upon HelD release, restart transcription. Our results provide insights into the architecture and regulation of the highly medically-relevant mycobacterial transcription machinery and define HelD as a clearing factor that releases RNAP from nonfunctional complexes with nucleic acids.
| + | |
| - | | + | |
| - | Mycobacterial HelD is a nucleic acids-clearing factor for RNA polymerase.,Kouba T, Koval' T, Sudzinova P, Pospisil J, Brezovska B, Hnilicova J, Sanderova H, Janouskova M, Sikova M, Halada P, Sykora M, Barvik I, Novacek J, Trundova M, Duskova J, Skalova T, Chon U, Murakami KS, Dohnalek J, Krasny L Nat Commun. 2020 Dec 18;11(1):6419. doi: 10.1038/s41467-020-20158-4. PMID:33339823<ref>PMID:33339823</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 6vsx" style="background-color:#fffaf0;"></div>
| + | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Vibrio subtilis ehrenberg 1835]] | + | [[Category: Bacillus subtilis]] |
| - | [[Category: DNA helicase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chon, U]] | + | [[Category: Chon U]] |
| - | [[Category: Murakami, K S]] | + | [[Category: Murakami KS]] |
| - | [[Category: Helicase]]
| + | |
| - | [[Category: Rna polymerase]]
| + | |
| - | [[Category: Transcription]]
| + | |
