6jyx: Difference between revisions

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OCA

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-'''Unreleased structure'''
-The entry 6jyx is ON HOLD
+==Structure of CbpJ from Streptococcus Pneumoniae TIGR4==
+<StructureSection load='6jyx' size='340' side='right'caption='[[6jyx]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6jyx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae_TIGR4 Streptococcus pneumoniae TIGR4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JYX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JYX 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]] 2&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CHT:CHOLINE+ION'>CHT</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=6jyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jyx OCA], [https://pdbe.org/6jyx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jyx RCSB], [https://www.ebi.ac.uk/pdbsum/6jyx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jyx ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/A0A0H2UNH0_STRPN A0A0H2UNH0_STRPN]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The choline-binding proteins play essential roles in pneumococcal colonization and virulence. It has been suggested that the choline-binding protein J (termed CbpJ; encoded by the gene sp_0378) from Streptococcus pneumoniae TIGR4 involves in the colonization in host and contributes to evasion of neutrophil killing. Here we report the 2.0A crystal structure of CbpJ in complex with choline. CbpJ consists of an N-terminal putative functional domain (N-domain) followed by a C-terminal choline-binding domain (CBD). The N-domain harbors four degenerated choline-binding repeats (CBRs) that lose the capacity of binding to choline, whereas the CBD is composed of seven typical CBRs. Further functional assays showed that the CBD contributes to the pneumococcal adhesion to human lung epithelial cell A549. These findings provide insights into the pneumococcal pathogenesis and broaden our understanding on the functions of choline-binding proteins.
-Authors:
+Crystal structure of the choline-binding protein CbpJ from Streptococcus pneumoniae.,Xu Q, Zhang JW, Chen Y, Li Q, Jiang YL Biochem Biophys Res Commun. 2019 May 16. pii: S0006-291X(19)30921-0. doi:, 10.1016/j.bbrc.2019.05.053. PMID:31104766<ref>PMID:31104766</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6jyx" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Streptococcus pneumoniae TIGR4]]
+[[Category: Jiang YL]]
+[[Category: Li Q]]
+[[Category: Xu Q]]
+[[Category: Zhang JW]]