5h3x

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<StructureSection load='5h3x' size='340' side='right'caption='[[5h3x]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='5h3x' size='340' side='right'caption='[[5h3x]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5h3x]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43765 Atcc 43765]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H3X OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5H3X FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5h3x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_suis Streptococcus suis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H3X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5H3X FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5h3w|5h3w]]</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]] 2.1&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fbps ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1307 ATCC 43765])</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=5h3x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h3x OCA], [https://pdbe.org/5h3x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5h3x RCSB], [https://www.ebi.ac.uk/pdbsum/5h3x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5h3x ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5h3x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h3x OCA], [http://pdbe.org/5h3x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h3x RCSB], [http://www.ebi.ac.uk/pdbsum/5h3x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h3x ProSAT]</span></td></tr>
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</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/RQCH_STRSY RQCH_STRSY] Part of the ribosome quality control system (RQC). Recruits Ala-charged tRNA and directs the elongation of stalled nascent chains on 50S ribosomal subunits, leading to non-templated C-terminal Ala extensions (Ala tail). The Ala tail promotes nascent chain degradation. May add between 1 and at least 8 Ala residues. Binds to stalled 50S ribosomal subunits.[HAMAP-Rule:MF_00844]
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The anchorless fibronectin-binding proteins (FnBPs) are a group of important virulence factors for which the structures are not available and the functions are not well defined. In this study we performed comprehensive studies on a prototypic member of this group: the fibronectin-/fibrinogen-binding protein from Streptococcus suis (FBPS). The structures of the N- and C-terminal halves (FBPS-N and FBPS-C), which together cover the full-length protein in sequence, were solved at a resolution of 2.1 and 2.6 A, respectively, and each was found to be composed of two domains with unique folds. Furthermore, we have elucidated the organization of these domains by small-angle X-ray scattering. We further showed that the fibronectin-binding site is located in FBPS-C and that FBPS promotes the adherence of S suis to host cells by attaching the bacteria via FBPS-N. Finally, we demonstrated that FBPS functions both as an adhesin, promoting S suis attachment to host cells, and as a bacterial factor, activating signaling pathways via beta1 integrin receptors to induce chemokine production.
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Structural and functional analysis of an anchorless fibronectin-binding protein FBPS from Gram-positive bacterium Streptococcus suis.,Musyoki AM, Shi Z, Xuan C, Lu G, Qi J, Gao F, Zheng B, Zhang Q, Li Y, Haywood J, Liu C, Yan J, Shi Y, Gao GF Proc Natl Acad Sci U S A. 2016 Nov 29;113(48):13869-13874. Epub 2016 Nov 10. PMID:27834729<ref>PMID:27834729</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 5h3x" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 43765]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Gao, G F]]
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[[Category: Streptococcus suis]]
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[[Category: MokiMusyoki, A]]
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[[Category: Gao GF]]
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[[Category: Qi, J]]
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[[Category: MokiMusyoki A]]
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[[Category: Cell adhesion]]
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[[Category: Qi J]]
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[[Category: Fibronectin-binding property]]
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Current revision

The structure of the N-terminal of the fibronectin/fibrinogen-binding protein from Streptococcus suis (FBPS)

PDB ID 5h3x

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