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| | <StructureSection load='7l0o' size='340' side='right'caption='[[7l0o]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='7l0o' size='340' side='right'caption='[[7l0o]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[7l0o]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_10558 Atcc 10558]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7L0O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7L0O FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7l0o]] is a 2 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=7L0O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7L0O 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]] 2.7Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2woy|2woy]]</div></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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ssp5, sspB ([https://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=7l0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7l0o OCA], [https://pdbe.org/7l0o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7l0o RCSB], [https://www.ebi.ac.uk/pdbsum/7l0o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7l0o 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=7l0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7l0o OCA], [https://pdbe.org/7l0o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7l0o RCSB], [https://www.ebi.ac.uk/pdbsum/7l0o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7l0o ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/SSP5_STRGN SSP5_STRGN]] May bind sialic acid residues of salivary agglutinin (SAG) in a calcium-dependent reaction. The interaction of SAG with its receptor in various oral streptococci modulate bacterial colonization of oral tissue and is associated with reduced levels of dental caries.
| + | [https://www.uniprot.org/uniprot/SSPB_STRGN SSPB_STRGN] May bind sialic acid residues of salivary agglutinin (SAG) in a calcium-dependent reaction. The interaction of SAG with its receptor in various oral streptococci modulate bacterial colonization of oral tissue and is associated with reduced levels of dental caries. |
| | <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: Deivanayagam, C]] | |
| - | [[Category: Schormann, N]] | |
| - | [[Category: Agglutinin receptor]] | |
| - | [[Category: C-terminal domain]] | |
| - | [[Category: Cell adhesion]] | |
| - | [[Category: Sspb]] | |
| | [[Category: Streptococcus gordonii]] | | [[Category: Streptococcus gordonii]] |
| | + | [[Category: Deivanayagam C]] |
| | + | [[Category: Schormann N]] |
| Structural highlights
Function
SSPB_STRGN May bind sialic acid residues of salivary agglutinin (SAG) in a calcium-dependent reaction. The interaction of SAG with its receptor in various oral streptococci modulate bacterial colonization of oral tissue and is associated with reduced levels of dental caries.
Publication Abstract from PubMed
Streptococcus gordonii is a member of the viridans streptococci and is an early colonizer of the tooth surface. Adherence to the tooth surface is enabled by proteins present on the S. gordonii cell surface, among which SspB belongs to one of the most well studied cell-wall-anchored adhesin families: the antigen I/II (AgI/II) family. The C-terminal region of SspB consists of three tandemly connected individual domains that display the DEv-IgG fold. These C-terminal domains contain a conserved Ca(2+)-binding site and isopeptide bonds, and they adhere to glycoprotein 340 (Gp340; also known as salivary agglutinin, SAG). Here, the structural and functional characterization of the C123(SspB) domain at 2.7 A resolution is reported. Although the individual C-terminal domains of Streptococcus mutans AgI/II and S. gordonii SspB show a high degree of both sequence and structural homology, superposition of these structures highlights substantial differences in their electrostatic surface plots, and this can be attributed to the relative orientation of the individual domains (C1, C2 and C3) with respect to each other and could reflect their specificity in binding to extracellular matrix molecules. Studies further confirmed that affinity for Gp340 or its scavenger receptor cysteine-rich (SRCR) domains requires two of the three domains of C123(SspB), namely C12 or C23, which is different from AgI/II. Using protein-protein docking studies, models for this observed functional difference between C123(SspB) and C123(AgI/II) in their binding to SRCR1 are presented.
Structural and functional analysis of the C-terminal region of Streptococcus gordonii SspB.,Schormann N, Purushotham S, Mieher JL, Patel M, Wu H, Deivanayagam C Acta Crystallogr D Struct Biol. 2021 Sep 1;77(Pt 9):1206-1215. doi:, 10.1107/S2059798321008135. Epub 2021 Aug 27. PMID:34473090[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Schormann N, Purushotham S, Mieher JL, Patel M, Wu H, Deivanayagam C. Structural and functional analysis of the C-terminal region of Streptococcus gordonii SspB. Acta Crystallogr D Struct Biol. 2021 Sep 1;77(Pt 9):1206-1215. doi:, 10.1107/S2059798321008135. Epub 2021 Aug 27. PMID:34473090 doi:http://dx.doi.org/10.1107/S2059798321008135
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