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| | ==Toxin-Antitoxin complex from Streptococcus pneumoniae== | | ==Toxin-Antitoxin complex from Streptococcus pneumoniae== |
| - | <StructureSection load='5yrz' size='340' side='right' caption='[[5yrz]], [[Resolution|resolution]] 2.30Å' scene=''> | + | <StructureSection load='5yrz' size='340' side='right'caption='[[5yrz]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5yrz]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Strpn Strpn]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YRZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YRZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5yrz]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae_TIGR4 Streptococcus pneumoniae TIGR4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YRZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YRZ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.304Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SP_1786 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=170187 STRPN]), SP_1787 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=170187 STRPN])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=5yrz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yrz OCA], [http://pdbe.org/5yrz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yrz RCSB], [http://www.ebi.ac.uk/pdbsum/5yrz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yrz 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=5yrz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yrz OCA], [https://pdbe.org/5yrz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yrz RCSB], [https://www.ebi.ac.uk/pdbsum/5yrz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yrz ProSAT]</span></td></tr> |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/A0A0H2URC7_STRPN A0A0H2URC7_STRPN] |
| - | Streptococcus pneumonia has attracted increasing attention due to its resistance to existing antibiotics. TA systems are essential for bacterial persistence under stressful conditions such as nutrient deprivation, antibiotic treatment, and immune system attacks. In particular, S. pneumoniae expresses the HicBA TA gene, which encodes the stable HicA toxin and the labile HicB antitoxin. These proteins interact to form a non-toxic TA complex under normal conditions, but the toxin is activated by release from the antitoxin in response to unfavorable growth conditions. Here, we present the first crystal structure showing the complete conformation of the HicBA complex from S. pneumonia. The structure reveals that the HicA toxin contains a double-stranded RNA-binding domain that is essential for RNA recognition and that the C-terminus of the HicB antitoxin folds into a ribbon-helix-helix DNA-binding motif. The active site of HicA is sterically blocked by the N-terminal region of HicB. RNase activity assays show that His36 is essential for the ribonuclease activity of HicA, and nuclear magnetic resonance (NMR) spectra show that several residues of HicB participate in binding to the promoter DNA of the HicBA operon. A toxin-mimicking peptide that inhibits TA complex formation and thereby increases toxin activity was designed, providing a novel approach to the development of new antibiotics.
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| - | Functional insights into the Streptococcus pneumoniae HicBA toxin-antitoxin system based on a structural study.,Kim DH, Kang SM, Park SJ, Jin C, Yoon HJ, Lee BJ Nucleic Acids Res. 2018 Jun 6. pii: 5033530. doi: 10.1093/nar/gky469. PMID:29878152<ref>PMID:29878152</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 5yrz" style="background-color:#fffaf0;"></div>
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| - | == References ==
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| - | <references/>
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Strpn]] | + | [[Category: Large Structures]] |
| - | [[Category: Kang, S M]] | + | [[Category: Streptococcus pneumoniae TIGR4]] |
| - | [[Category: Kim, D H]] | + | [[Category: Kang SM]] |
| - | [[Category: Antitoxin]] | + | [[Category: Kim DH]] |
| - | [[Category: Antitoxin-hydrolase complex]]
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| - | [[Category: Dna]]
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| - | [[Category: Hydrolase]]
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| - | [[Category: Toxin]]
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