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| ==Crystal structure of dimeric latent PorU from Porphyromonas gingivalis== | | ==Crystal structure of dimeric latent PorU from Poprhyromonas gingivalis== |
| <StructureSection load='6za2' size='340' side='right'caption='[[6za2]], [[Resolution|resolution]] 3.35Å' scene=''> | | <StructureSection load='6za2' size='340' side='right'caption='[[6za2]], [[Resolution|resolution]] 3.35Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[6za2]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZA2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZA2 FirstGlance]. <br> | | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZA2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZA2 FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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]] 3.35Å</td></tr> |
| | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=6za2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6za2 OCA], [https://pdbe.org/6za2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6za2 RCSB], [https://www.ebi.ac.uk/pdbsum/6za2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6za2 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=6za2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6za2 OCA], [https://pdbe.org/6za2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6za2 RCSB], [https://www.ebi.ac.uk/pdbsum/6za2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6za2 ProSAT]</span></td></tr> |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Porphyromonas gingivalis is a keystone pathogen of the human dysbiotic oral microbiome that causes severe periodontitis. It employs a type-IX secretion system (T9SS) to shuttle proteins across the outer membrane (OM) for virulence. Uniquely, T9SS cargoes carry a C-terminal domain (CTD) as a secretion signal, which is cleaved and replaced with anionic lipopolysaccharide by transpeptidation for extracellular anchorage to the OM. Both reactions are carried out by PorU, the only known dual-function, C-terminal signal peptidase and sortase. PorU is itself secreted by the T9SS, but its CTD is not removed; instead, intact PorU combines with PorQ, PorV, and PorZ in the OM-inserted "attachment complex." Herein, we revealed that PorU transits between active monomers and latent dimers and solved the crystal structure of the approximately 260-kDa dimer. PorU has an elongated shape approximately 130 A in length and consists of seven domains. The first three form an intertwined N-terminal cluster likely engaged in substrate binding. They are followed by a gingipain-type catalytic domain (CD), two immunoglobulin-like domains (IGL), and the CTD. In the first IGL, a long "latency beta-hairpin" protrudes approximately 30 A from the surface to form an intermolecular beta-barrel with beta-strands from the symmetric CD, which is in a latent conformation. Homology modeling of the competent CD followed by in vivo validation through a cohort of mutant strains revealed that PorU is transported and functions as a monomer through a C(690)/H(657) catalytic dyad. Thus, dimerization is an intermolecular mechanism for PorU regulation to prevent untimely activity until joining the attachment complex.
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| Intermolecular latency regulates the essential C-terminal signal peptidase and sortase of the Porphyromonas gingivalis type-IX secretion system.,Mizgalska D, Goulas T, Rodriguez-Banqueri A, Veillard F, Madej M, Malecka E, Szczesniak K, Ksiazek M, Widziolek M, Guevara T, Eckhard U, Sola M, Potempa J, Gomis-Ruth FX Proc Natl Acad Sci U S A. 2021 Oct 5;118(40). pii: 2103573118. doi:, 10.1073/pnas.2103573118. Epub 2021 Sep 30. PMID:34593635<ref>PMID:34593635</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 6za2" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Gomis-Ruth, F X]] | | [[Category: Gomis-Ruth FX]] |
| [[Category: Goulas, T]] | | [[Category: Goulas T]] |
| [[Category: Guevara, T]] | | [[Category: Guevara T]] |
| [[Category: Potempa, J]] | | [[Category: Potempa J]] |
| [[Category: Rodriguez-Banqueri, A]] | | [[Category: Rodriguez-Banqueri A]] |
| [[Category: Hydrolase]]
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| [[Category: Periodontopathogen]]
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| [[Category: Sortase]]
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| [[Category: Transpeptidase]]
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| [[Category: Type-ix secretion system]]
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| [[Category: Virulence factor]]
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