6efi: Difference between revisions

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'''Unreleased structure'''


The entry 6efi is ON HOLD
==SK678 binding region (Siglec + Unique)==
<StructureSection load='6efi' size='340' side='right'caption='[[6efi]], [[Resolution|resolution]] 1.71&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6efi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_sanguinis_SK678 Streptococcus sanguinis SK678]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EFI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6EFI FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.715&#8491;</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>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=6efi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6efi OCA], [https://pdbe.org/6efi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6efi RCSB], [https://www.ebi.ac.uk/pdbsum/6efi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6efi ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/F0FS71_STRSA F0FS71_STRSA]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacterial binding to host receptors underlies both commensalism and pathogenesis. Many streptococci adhere to protein-attached carbohydrates expressed on cell surfaces using Siglec-like binding regions (SLBRs). The precise glycan repertoire recognized may dictate whether the organism is a strict commensal versus a pathogen. However, it is currently not clear what drives receptor selectivity. Here, we use five representative SLBRs and identify regions of the receptor binding site that are hypervariable in sequence and structure. We show that these regions control the identity of the preferred carbohydrate ligand using chimeragenesis and single amino acid substitutions. We further evaluate how the identity of the preferred ligand affects the interaction with glycoprotein receptors in human saliva and plasma samples. As point mutations can change the preferred human receptor, these studies suggest how streptococci may adapt to changes in the environmental glycan repertoire.


Authors: Iverson, T.M.
Origins of glycan selectivity in streptococcal Siglec-like adhesins suggest mechanisms of receptor adaptation.,Bensing BA, Stubbs HE, Agarwal R, Yamakawa I, Luong K, Solakyildirim K, Yu H, Hadadianpour A, Castro MA, Fialkowski KP, Morrison KM, Wawrzak Z, Chen X, Lebrilla CB, Baudry J, Smith JC, Sullam PM, Iverson TM Nat Commun. 2022 May 18;13(1):2753. doi: 10.1038/s41467-022-30509-y. PMID:35585145<ref>PMID:35585145</ref>


Description: SK678
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Iverson, T.M]]
<div class="pdbe-citations 6efi" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptococcus sanguinis SK678]]
[[Category: Iverson TM]]

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