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| | <StructureSection load='5vaf' size='340' side='right'caption='[[5vaf]], [[Resolution|resolution]] 2.77Å' scene=''> | | <StructureSection load='5vaf' size='340' side='right'caption='[[5vaf]], [[Resolution|resolution]] 2.77Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5vaf]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_10558 Atcc 10558]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VAF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VAF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5vaf]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_gordonii Streptococcus gordonii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VAF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VAF FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5vae|5vae]]</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]] 2.771Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">asp1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1302 ATCC 10558])</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=5vaf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vaf OCA], [https://pdbe.org/5vaf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vaf RCSB], [https://www.ebi.ac.uk/pdbsum/5vaf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vaf ProSAT]</span></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=5vaf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vaf OCA], [http://pdbe.org/5vaf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vaf RCSB], [http://www.ebi.ac.uk/pdbsum/5vaf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vaf ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/ASP1_STRGN ASP1_STRGN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 10558]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chen, Y]] | + | [[Category: Streptococcus gordonii]] |
| - | [[Category: Jeffrey, P D]] | + | [[Category: Chen Y]] |
| - | [[Category: Rapoport, T A]] | + | [[Category: Jeffrey PD]] |
| - | [[Category: Accessory secretion]] | + | [[Category: Rapoport TA]] |
| - | [[Category: Bacterial adhesin]]
| + | |
| - | [[Category: Cell adhesion]]
| + | |
| - | [[Category: O-glycosylation]]
| + | |
| Structural highlights
Function
ASP1_STRGN
Publication Abstract from PubMed
Many pathogenic bacteria, including Streptococcus gordonii, possess a pathway for the cellular export of a single serine-rich-repeat protein that mediates the adhesion of bacteria to host cells and the extracellular matrix. This adhesin protein is O-glycosylated by several cytosolic glycosyltransferases and requires three accessory Sec proteins (Asp1-3) for export, but how the adhesin protein is processed for export is not well understood. Here, we report that the S. gordonii adhesin GspB is sequentially O-glycosylated by three enzymes (GtfA/B, Nss, and Gly) that attach N-acetylglucosamine and glucose to Ser/Thr residues. We also found that modified GspB is transferred from the last glycosyltransferase to the Asp1/2/3 complex. Crystal structures revealed that both Asp1 and Asp3 are related to carbohydrate-binding proteins, suggesting that they interact with carbohydrates and bind glycosylated adhesin, a notion that was supported by further analyses. We further observed that Asp1 also has an affinity for phospholipids, which is attenuated by Asp2. In summary, our findings support a model in which the GspB adhesin is sequentially glycosylated by GtfA/B, Nss, and Gly and then transferred to the Asp1/2/3 complex in which Asp1 mediates the interaction of the Asp1/2/3 complex with the lipid bilayer for targeting of matured GspB to the export machinery.
Unraveling the sequence of cytosolic reactions in the export of GspB adhesin from Streptococcus gordonii.,Chen Y, Bensing BA, Seepersaud R, Mi W, Liao M, Jeffrey PD, Shajahan A, Sonon RN, Azadi P, Sullam PM, Rapoport TA J Biol Chem. 2018 Feb 9. pii: RA117.000963. doi: 10.1074/jbc.RA117.000963. PMID:29462788[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chen Y, Bensing BA, Seepersaud R, Mi W, Liao M, Jeffrey PD, Shajahan A, Sonon RN, Azadi P, Sullam PM, Rapoport TA. Unraveling the sequence of cytosolic reactions in the export of GspB adhesin from Streptococcus gordonii. J Biol Chem. 2018 Feb 9. pii: RA117.000963. doi: 10.1074/jbc.RA117.000963. PMID:29462788 doi:http://dx.doi.org/10.1074/jbc.RA117.000963
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