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| | <StructureSection load='5dl2' size='340' side='right'caption='[[5dl2]], [[Resolution|resolution]] 3.50Å' scene=''> | | <StructureSection load='5dl2' size='340' side='right'caption='[[5dl2]], [[Resolution|resolution]] 3.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5dl2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptococcus_pyogenes_mgas10870 Streptococcus pyogenes mgas10870]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DL2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DL2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5dl2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pyogenes_MGAS10870 Streptococcus pyogenes MGAS10870]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DL2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DL2 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rgg ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=530008 Streptococcus pyogenes MGAS10870])</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]] 3.5Å</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=5dl2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dl2 OCA], [http://pdbe.org/5dl2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dl2 RCSB], [http://www.ebi.ac.uk/pdbsum/5dl2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5dl2 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=5dl2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dl2 OCA], [https://pdbe.org/5dl2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dl2 RCSB], [https://www.ebi.ac.uk/pdbsum/5dl2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dl2 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/D3KVD8_STRPY D3KVD8_STRPY] |
| - | Group A Streptococcus (GAS) is an exclusive human pathogen that causes significant disease burden. Global regulator RopB of GAS controls the expression of several major virulence factors including secreted protease SpeB during high cell density. However, the molecular mechanism for RopB-dependent speB expression remains unclear. To understand the mechanism of transcription activation by RopB, we determined the crystal structure of the C-terminal domain of RopB. RopB-CTD has the TPR motif, a signature motif involved in protein-peptide interactions and shares significant structural homology with the quorum sensing RRNPP family regulators. Characterization of the high cell density-specific cell-free growth medium demonstrated the presence of a low molecular weight proteinaceous secreted factor that upregulates RopB-dependent speB expression. Together, these results suggest that RopB and its cognate peptide signals constitute an intercellular signaling machinery that controls the virulence gene expression in concert with population density. Structure-guided mutational analyses of RopB dimer interface demonstrated that single alanine substitutions at this critical interface significantly altered RopB-dependent speB expression and attenuated GAS virulence. Results presented here suggested that a properly aligned RopB dimer interface is important for GAS pathogenesis and highlighted the dimerization interactions as a plausible therapeutic target for the development of novel antimicrobials. This article is protected by copyright. All rights reserved.
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| - | Structural and functional analysis of RopB - a major virulence regulator in Streptococcus pyogenes.,Makthal N, Gavagan M, Do H, Olsen RJ, Musser JM, Kumaraswami M Mol Microbiol. 2015 Dec 29. doi: 10.1111/mmi.13294. PMID:26714274<ref>PMID:26714274</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 5dl2" style="background-color:#fffaf0;"></div>
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| - | == References ==
| + | |
| - | <references/>
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Streptococcus pyogenes mgas10870]] | + | [[Category: Streptococcus pyogenes MGAS10870]] |
| - | [[Category: Kumaraswami, M]] | + | [[Category: Kumaraswami M]] |
| - | [[Category: Bacterial pathogenesis]]
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| - | [[Category: Tetratricopeptide repeat]]
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| - | [[Category: Transcription regulator]]
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| - | [[Category: Virulence]]
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| - | [[Category: Virulence regulation]]
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