View source for 3wi5


==Crystal structure of the Loop 7 mutant PorB from Neisseria meningitidis serogroup B==
<StructureSection load='3wi5' size='340' side='right'caption='[[3wi5]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3wi5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WI5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WI5 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]] 2.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</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=3wi5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wi5 OCA], [https://pdbe.org/3wi5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wi5 RCSB], [https://www.ebi.ac.uk/pdbsum/3wi5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wi5 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/OMPB1_NEIMB OMPB1_NEIMB] Serves as a slightly cation selective porin.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Among all Neisseriae species, Neisseria meningitidis and Neisseria gonorrhoeae are the only human pathogens, causative agents of bacterial meningitis and gonorrhoea, respectively. PorB, a pan-Neisseriae trimeric porin that mediates diffusive transport of essential molecules across the bacterial outer membrane, is also known to activate host innate immunity via Toll-like receptor 2 (TLR2)-mediated signaling. The molecular mechanism of PorB binding to TLR2 is not known, but it has been hypothesized that electrostatic interactions contribute to ligand/receptor binding. Strain-specific sequence variability in the surface-exposed loops of PorB which are potentially implicated in TLR2 binding, may explain the difference in TLR2-mediated cell activation in vitro by PorB homologs from the commensal Neisseriae lactamica and the pathogen N. meningitidis. Here, we report a comparative structural analysis of PorB from N. meningitidis serogroup B strain 8765 (63% sequence homology with PorB from N. meningitidis serogroup W135) and a mutant in which amino acid substitutions in the extracellular loop 7 lead to significantly reduced TLR2-dependent activity in vitro. We observe that this mutation both alters the loop conformation and causes dramatic changes of electrostatic surface charge, both of which may affect TLR2 recognition and signaling.

Crystallographic analysis of Neisseria meningitidis PorB extracellular loops potentially implicated in TLR2 recognition.,Kattner C, Toussi DN, Zaucha J, Wetzler LM, Ruppel N, Zachariae U, Massari P, Tanabe M J Struct Biol. 2014 Mar;185(3):440-7. doi: 10.1016/j.jsb.2013.12.006. Epub 2013, Dec 19. PMID:24361688<ref>PMID:24361688</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3wi5" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Neisseria meningitidis]]
[[Category: Kattner C]]
[[Category: Massari P]]
[[Category: Ruppel N]]
[[Category: Tanabe M]]
[[Category: Toussi D]]
[[Category: Wetzler LM]]