6sj9
From Proteopedia
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<StructureSection load='6sj9' size='340' side='right'caption='[[6sj9]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='6sj9' size='340' side='right'caption='[[6sj9]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6sj9]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SJ9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6SJ9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6sj9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_13344 Atcc 13344]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SJ9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6SJ9 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AAur_2182 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=43663 ATCC 13344])</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=6sj9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sj9 OCA], [http://pdbe.org/6sj9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6sj9 RCSB], [http://www.ebi.ac.uk/pdbsum/6sj9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6sj9 ProSAT]</span></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=6sj9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sj9 OCA], [http://pdbe.org/6sj9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6sj9 RCSB], [http://www.ebi.ac.uk/pdbsum/6sj9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6sj9 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | In mycobacteria, transcriptional activator PafBC is responsible for upregulating the majority of genes induced by DNA damage. Understanding the mechanism of PafBC activation is impeded by a lack of structural information on this transcription factor that contains a widespread, but poorly understood WYL domain frequently encountered in bacterial transcription factors. Here, we determine the crystal structure of Arthrobacter aurescens PafBC. The protein consists of two modules, each harboring an N-terminal helix-turn-helix DNA-binding domain followed by a central WYL and a C-terminal extension (WCX) domain. The WYL domains exhibit Sm-folds, while the WCX domains adopt ferredoxin-like folds, both characteristic for RNA-binding proteins. Our results suggest a mechanism of regulation in which WYL domain-containing transcription factors may be activated by binding RNA or other nucleic acid molecules. Using an in vivo mutational screen in Mycobacterium smegmatis, we identify potential co-activator binding sites on PafBC. | ||
| + | |||
| + | Structure and functional implications of WYL domain-containing bacterial DNA damage response regulator PafBC.,Muller AU, Leibundgut M, Ban N, Weber-Ban E Nat Commun. 2019 Oct 11;10(1):4653. doi: 10.1038/s41467-019-12567-x. PMID:31604936<ref>PMID:31604936</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6sj9" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Atcc 13344]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Ban, N]] | [[Category: Ban, N]] | ||
Revision as of 08:15, 23 October 2019
Proteasome accessory factor B/C (PafBC) of Arthrobacter aurescens
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