5vae
From Proteopedia
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<StructureSection load='5vae' size='340' side='right' caption='[[5vae]], [[Resolution|resolution]] 3.11Å' scene=''> | <StructureSection load='5vae' size='340' side='right' caption='[[5vae]], [[Resolution|resolution]] 3.11Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5vae]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VAE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VAE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5vae]] is a 8 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=5VAE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VAE FirstGlance]. <br> |
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5vaf|5vaf]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5vaf|5vaf]]</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]), asp3 ([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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5vae FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vae OCA], [http://pdbe.org/5vae PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vae RCSB], [http://www.ebi.ac.uk/pdbsum/5vae PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vae 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=5vae FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vae OCA], [http://pdbe.org/5vae PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vae RCSB], [http://www.ebi.ac.uk/pdbsum/5vae PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vae ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:29462788</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5vae" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Atcc 10558]] | ||
[[Category: Chen, Y]] | [[Category: Chen, Y]] | ||
[[Category: Jeffrey, P D]] | [[Category: Jeffrey, P D]] | ||
Revision as of 07:10, 28 February 2018
Crystal structure of accessory secretion protein 1 and 3
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