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| | ==IgA1 Protease G5 domain structure== | | ==IgA1 Protease G5 domain structure== |
| - | <StructureSection load='6oh1' size='340' side='right'caption='[[6oh1]], [[NMR_Ensembles_of_Models | 8 NMR models]]' scene=''> | + | <StructureSection load='6oh1' size='340' side='right'caption='[[6oh1]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6oh1]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OH1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OH1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6oh1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OH1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OH1 FirstGlance]. <br> |
| - | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/IgA-specific_metalloendopeptidase IgA-specific metalloendopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.13 3.4.24.13] </span></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=6oh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oh1 OCA], [http://pdbe.org/6oh1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6oh1 RCSB], [http://www.ebi.ac.uk/pdbsum/6oh1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6oh1 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=6oh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oh1 OCA], [https://pdbe.org/6oh1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6oh1 RCSB], [https://www.ebi.ac.uk/pdbsum/6oh1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6oh1 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/IGA1B_STREE IGA1B_STREE] |
| - | Many bacterial pathogens express small G5 domains that exist in the context of various membrane-anchored proteins and these G5 domains have been associated with colonization, cellular adhesion, and biofilm formation. However, despite over a decade since the computational prediction of these G5 domains, many remain uncharacterized, particularly those from Streptococcus pneumoniae. Of five previously predicted G5 domains we found that four of these, all derived from S. pneumoniae, are independently folded modules. As one of these exhibits extreme line broadening due to self-association, we were able to use NMR solution studies to probe the potential ligand interactions of the remaining three G5 domains. None of these G5 domains engage N-acetylglucosamine (NAG) as previously predicted but do interact with other small molecules that may modulate adherence to both bacteria and host cells. Specifically, while all G5 domains tested engage Zn, only one of these G5 domains engage heparin. NMR solution structural studies of the IgA1 Protease G5 (IgA1P-G5) and endo-beta-N-acetylglucosaminidase-D G5 (ENDD-G5) also facilitated identification of the ligand binding sites and confirm the typical G5 fold that comprises two connected beta-sheets with no canonical core. NMR relaxation experiments indicate flexibility on both ends and within the connecting regions between the beta-sheets. Our studies thus establish a basis for future biological experiments to test whether the ligands presented here are involved in bacterial adherence, either to bacteria or to host cells.
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| - | Streptococcus pneumoniae G5 domains bind different ligands.,Paukovich N, Redzic JS, Chi YC, Rahkola JT, Issaian A, Blue A, Hansen KC, Janoff EN, Eisenmesser EZ Protein Sci. 2019 Oct;28(10):1797-1805. doi: 10.1002/pro.3693. Epub 2019 Aug 9. PMID:31390088<ref>PMID:31390088</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 6oh1" style="background-color:#fffaf0;"></div>
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| - | == References ==
| + | |
| - | <references/>
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: IgA-specific metalloendopeptidase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chi, Y C]] | + | [[Category: Streptococcus pneumoniae]] |
| - | [[Category: Eisenmesser, E Z]] | + | [[Category: Chi YC]] |
| - | [[Category: Janoff, E N]] | + | [[Category: Eisenmesser EZ]] |
| - | [[Category: Paukovich, N]] | + | [[Category: Janoff EN]] |
| - | [[Category: Rahkola, J T]] | + | [[Category: Paukovich N]] |
| - | [[Category: Redzic, J S]] | + | [[Category: Rahkola JT]] |
| - | [[Category: G5 domain]]
| + | [[Category: Redzic JS]] |
| - | [[Category: Hydrolase]]
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| - | [[Category: Iga1]]
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| - | [[Category: Protease]]
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