View source for 5nxk


==L. reuteri 53608 SRRP==
<StructureSection load='5nxk' size='340' side='right'caption='[[5nxk]], [[Resolution|resolution]] 1.92&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5nxk]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Limosilactobacillus_reuteri_subsp._suis Limosilactobacillus reuteri subsp. suis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NXK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NXK 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]] 1.918&#8491;</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=5nxk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nxk OCA], [https://pdbe.org/5nxk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nxk RCSB], [https://www.ebi.ac.uk/pdbsum/5nxk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nxk ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Lactobacillus reuteri, a Gram-positive bacterial species inhabiting the gastrointestinal tract of vertebrates, displays remarkable host adaptation. Previous mutational analyses of rodent strain L. reuteri 100-23C identified a gene encoding a predicted surface-exposed serine-rich repeat protein (SRRP100-23) that was vital for L. reuteri biofilm formation in mice. SRRPs have emerged as an important group of surface proteins on many pathogens, but no structural information is available in commensal bacteria. Here we report the 2.00-A and 1.92-A crystal structures of the binding regions (BRs) of SRRP100-23 and SRRP53608 from L. reuteri ATCC 53608, revealing a unique beta-solenoid fold in this important adhesin family. SRRP53608-BR bound to host epithelial cells and DNA at neutral pH and recognized polygalacturonic acid (PGA), rhamnogalacturonan I, or chondroitin sulfate A at acidic pH. Mutagenesis confirmed the role of the BR putative binding site in the interaction of SRRP53608-BR with PGA. Long molecular dynamics simulations showed that SRRP53608-BR undergoes a pH-dependent conformational change. Together, these findings provide mechanistic insights into the role of SRRPs in host-microbe interactions and open avenues of research into the use of biofilm-forming probiotics against clinically important pathogens.

Structural basis for the role of serine-rich repeat proteins from Lactobacillus reuteri in gut microbe-host interactions.,Sequeira S, Kavanaugh D, MacKenzie DA, Suligoj T, Walpole S, Leclaire C, Gunning AP, Latousakis D, Willats WGT, Angulo J, Dong C, Juge N Proc Natl Acad Sci U S A. 2018 Mar 5. pii: 1715016115. doi:, 10.1073/pnas.1715016115. PMID:29507249<ref>PMID:29507249</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Limosilactobacillus reuteri subsp. suis]]
[[Category: Dong C]]
[[Category: Sequeira S]]