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| ==Solution structure of KTI55== | | ==Solution structure of KTI55== |
| <StructureSection load='6bzk' size='340' side='right'caption='[[6bzk]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | | <StructureSection load='6bzk' size='340' side='right'caption='[[6bzk]]' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[6bzk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_scarlatinae"_klein_1884 "micrococcus scarlatinae" klein 1884]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BZK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BZK FirstGlance]. <br> | | <table><tr><td colspan='2'>[[6bzk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BZK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BZK FirstGlance]. <br> |
| </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">emm ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1314 "Micrococcus scarlatinae" Klein 1884])</td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=6bzk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bzk OCA], [http://pdbe.org/6bzk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bzk RCSB], [http://www.ebi.ac.uk/pdbsum/6bzk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bzk 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=6bzk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bzk OCA], [https://pdbe.org/6bzk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bzk RCSB], [https://www.ebi.ac.uk/pdbsum/6bzk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bzk ProSAT]</span></td></tr> |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
| | == Function == |
| == Publication Abstract from PubMed == | | [https://www.uniprot.org/uniprot/M4I070_STRPY M4I070_STRPY] |
| Group A Streptococcus pyogenes (GAS) is a causative agent of pharyngeal and dermal infections in humans. A major virulence determinant of GAS is its dimeric signature fibrillar M-protein (M-Prt), which is evolutionarily designed in modules, ranging from a hypervariable extracellular N-terminal region to a progressively more highly conserved C-terminus that is covalently anchored to the cell wall. Of the >250 GAS isolates classified, only the subset of skin-trophic Pattern D strains expresses a specific serotype of M-Prt, PAM, that directly binds to host human plasminogen (hPg) via its extracellular NH2-terminal variable A-domain region. This interaction allows these GAS strains to accumulate components of the host fibrinolytic system on their surfaces to serve extracellular functions. While structure-function studies have been accomplished on M-Prts from Pattern A-C GAS isolates with different direct ligand binding properties compared to PAM, much less is known regarding the structure-function relationships of PAM-type M-Prts, particularly their dimerization determinants. To examine these questions, PAMs from seven GAS strains with sequence variations in the NH2-terminal ligand binding domains, as well as truncated versions of PAM, were designed and studied. The results from bioinformatic and biophysical analyses show that the different domains of PAM are disparately engaged in dimerization. From these data, we propose an experimentally-based model for PAM secondary and quaternary structures that is highly dependent on the conserved helical C-terminal C-D-domains. In addition, while the N-terminal regions of PAMs are variable in sequence, the binding properties of hPg and its activated product, plasmin, to the A-domain, remain intact.
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| Contributions of different modules of the plasminogen-binding Streptococcus pyogenes M-protein that mediate its functional dimerization.,Qiu C, Yuan Y, Zajicek J, Liang Z, Balsara RD, Brito-Robionson T, Lee SW, Ploplis VA, Castellino FJ J Struct Biol. 2018 Nov;204(2):151-164. doi: 10.1016/j.jsb.2018.07.017. Epub 2018, Jul 30. PMID:30071314<ref>PMID:30071314</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 6bzk" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Micrococcus scarlatinae klein 1884]]
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| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Castellino, F J]] | | [[Category: Streptococcus pyogenes]] |
| [[Category: Qiu, C]] | | [[Category: Castellino FJ]] |
| [[Category: Yuan, Y]] | | [[Category: Qiu C]] |
| [[Category: Plasminogen binding peptide]] | | [[Category: Yuan Y]] |
| [[Category: Protein binding]]
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