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| | <StructureSection load='5y1a' size='340' side='right'caption='[[5y1a]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='5y1a' size='340' side='right'caption='[[5y1a]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5y1a]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_33277 Atcc 33277]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y1A OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5Y1A FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5y1a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Porphyromonas_gingivalis Porphyromonas gingivalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y1A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5Y1A FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HBP35, AT291_00855 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=837 ATCC 33277])</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]] 1.8Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5y1a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y1a OCA], [http://pdbe.org/5y1a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5y1a RCSB], [http://www.ebi.ac.uk/pdbsum/5y1a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5y1a 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=5y1a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y1a OCA], [https://pdbe.org/5y1a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5y1a RCSB], [https://www.ebi.ac.uk/pdbsum/5y1a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5y1a ProSAT]</span></td></tr> |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/Q8G962_PORGN Q8G962_PORGN] |
| - | The periodontal pathogen Porphyromonas gingivalis secretes many potent virulence factors using the type IX secretion system (T9SS). T9SS cargo proteins that have been structurally determined by X-ray crystallography are composed of a signal peptide, functional domain(s), an immunoglobulin (Ig)-like domain and a C-terminal domain. Role of the Ig-like domains of cargo proteins in the T9SS has not been elucidated. Gingipain proteases, which are cargo proteins of the T9SS, were degraded when their Ig-like domains were lacking or truncated. The degradation was dependent on the activity of a quality control factor, HtrA protease. Another T9SS cargo protein, HBP35, which has a thioredoxin domain as a functional domain, was analyzed by X-ray crystallography, revealing that HBP35 has an Ig-like domain after the thioredoxin domain and that the hydrophobic regions of the thioredoxin domain and the Ig-like domain face each other. HBP35 with substitution of hydrophobic amino acids in the Ig-like domain was degraded depending on HtrA. These results suggest that the Ig-like domain mediates stability of the cargo proteins in the T9SS.
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| - | Immunoglobulin-like domains of the cargo proteins are essential for protein stability during secretion by the type IX secretion system.,Sato K, Kakuda S, Yukitake H, Kondo Y, Shoji M, Takebe K, Narita Y, Naito M, Nakane D, Abiko Y, Hiratsuka K, Suzuki M, Nakayama K Mol Microbiol. 2018 Oct;110(1):64-81. doi: 10.1111/mmi.14083. Epub 2018 Oct 4. PMID:30030863<ref>PMID:30030863</ref>
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| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 5y1a" style="background-color:#fffaf0;"></div>
| + | |
| - | == References ==
| + | |
| - | <references/>
| + | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 33277]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kakuda, S]] | + | [[Category: Porphyromonas gingivalis]] |
| - | [[Category: Sato, K]] | + | [[Category: Kakuda S]] |
| - | [[Category: Suzuki, M]] | + | [[Category: Sato K]] |
| - | [[Category: Beta-sandwich domain]] | + | [[Category: Suzuki M]] |
| - | [[Category: Electron transport]]
| + | |
| - | [[Category: Porphyromonas gingivali]]
| + | |
| - | [[Category: Thioredoxin domain]]
| + | |
