View source for 5gt1


==crystal structure of cbpa from L. salivarius REN==
<StructureSection load='5gt1' size='340' side='right'caption='[[5gt1]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5gt1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ligilactobacillus_salivarius_str._Ren Ligilactobacillus salivarius str. Ren]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GT1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GT1 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]] 1.85&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=5gt1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gt1 OCA], [https://pdbe.org/5gt1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gt1 RCSB], [https://www.ebi.ac.uk/pdbsum/5gt1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gt1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0F7PV22_9LACO A0A0F7PV22_9LACO] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Lactobacillus salivarius REN, a novel probiotic isolated from Chinese centenarians, can adhere to intestinal epithelial cells and subsequently colonize the host. We show here that the surface-layer protein choline-binding protein A (CbpA) of L. salivarius REN was involved in adherence to the human colorectal adenocarcinoma cell line HT-29. Adhesion of a cbpA deletion mutant was significantly reduced compared with that of wild-type, suggesting that CbpA acts as an adhesin that mediates the interaction between the bacterium and its host. To identify the molecular mechanism of adhesion, we determined the crystal structure of a truncated form of CbpA that is likely involved in binding to its cell-surface receptor. The crystal structure identified CbpA as a peptidase of the M23 family whose members harbor a zinc-dependent catalytic site. Therefore, we propose that CbpA acts as a multifunctional surface protein that cleaves the host extracellular matrix and participates in adherence. Moreover, we identified enolase as the CbpA receptor on the surface of HT-29 cells. The present study reveals a new class of surface-layer proteins as well as the molecular mechanism that may contribute to the ability of L. salivarius REN to colonize the human gut.

The Adhesion of Lactobacillus salivarius REN to a Human Intestinal Epithelial Cell Line Requires S-layer Proteins.,Wang R, Jiang L, Zhang M, Zhao L, Hao Y, Guo H, Sang Y, Zhang H, Ren F Sci Rep. 2017 Mar 10;7:44029. doi: 10.1038/srep44029. PMID:28281568<ref>PMID:28281568</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5gt1" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Ligilactobacillus salivarius str. Ren]]
[[Category: Jiang L]]
[[Category: Ren F]]