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5uqz

From Proteopedia

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Current revision (14:28, 6 March 2024) (edit) (undo)
 
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<StructureSection load='5uqz' size='340' side='right'caption='[[5uqz]], [[Resolution|resolution]] 1.15&Aring;' scene=''>
<StructureSection load='5uqz' size='340' side='right'caption='[[5uqz]], [[Resolution|resolution]] 1.15&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5uqz]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Strmu Strmu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UQZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UQZ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5uqz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_mutans_UA159 Streptococcus mutans UA159]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UQZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UQZ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.149&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gbpC, SMU_1396 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210007 STRMU])</td></tr>
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<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>
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<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=5uqz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uqz OCA], [http://pdbe.org/5uqz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5uqz RCSB], [http://www.ebi.ac.uk/pdbsum/5uqz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5uqz ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5uqz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uqz OCA], [https://pdbe.org/5uqz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5uqz RCSB], [https://www.ebi.ac.uk/pdbsum/5uqz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5uqz ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q8DTF1_STRMU Q8DTF1_STRMU]
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The high-resolution structure of Glucan binding protein C (GbpC) at 1.14 A, a sucrose-dependent virulence factor of the dental caries pathogen Streptococcus mutans, has been determined. GbpC not only shares structural similarities with the V-regions of AgI/II and SspB, but also functional adherence to SAG and its scavenger receptor cysteine rich domains (SRCRs) which is not only a newly identified function for GbpC, but also an additional fail-safe binding mechanism for S. mutans Despite the structural similarities with S. mutans Antigen I/II (AgI/II) and SspB of Streptococcus gordonii, GbpC remains unique among these surface proteins in its propensity to adhere to dextran/glucans. The complex crystal structure of GbpC with dextrose (beta-D glucose, BGC) highlights exclusive structural features that facilitates this interaction with dextran. Targeted deletion mutant studies on GbpC's divergent loop region in the vicinity of a highly-conserved calcium binding site confirm its role in biofilm formation. Finally, we present a model for adherence to dextran. The structure of GbpC highlights how artfully microbes have engineered the lectin-like folds to broaden their functional adherence repertoire.
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Glucan Binding Protein C of Streptococcus mutans Mediates both Sucrose-Independent and Sucrose-Dependent Adherence.,Mieher JL, Larson MR, Schormann N, Purushotham S, Wu R, Rajashankar KR, Wu H, Deivanayagam C Infect Immun. 2018 Apr 23. pii: IAI.00146-18. doi: 10.1128/IAI.00146-18. PMID:29685986<ref>PMID:29685986</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5uqz" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Strmu]]
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[[Category: Streptococcus mutans UA159]]
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[[Category: Deivanayagam, C]]
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[[Category: Deivanayagam C]]
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[[Category: Larson, M R]]
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[[Category: Larson MR]]
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[[Category: Mieher, J]]
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[[Category: Mieher J]]
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[[Category: Purushotham, S]]
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[[Category: Purushotham S]]
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[[Category: Rajashankar, K R]]
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[[Category: Rajashankar KR]]
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[[Category: Wu, H]]
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[[Category: Wu H]]
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[[Category: Wu, R]]
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[[Category: Wu R]]
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[[Category: Beta-supersandwich]]
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[[Category: Glucan]]
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[[Category: Sugar binding]]
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[[Category: Sugar binding protein]]
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Current revision

Structural Analysis of the Glucan Binding Protein C of Streptococcus mutans Provides Evidence that it Mediates both Sucrose-Independent and -Dependent Adherence

PDB ID 5uqz

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