View source for 5ldv


==Crystal Structures of MOMP from Campylobacter jejuni==
<StructureSection load='5ldv' size='340' side='right'caption='[[5ldv]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5ldv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Campylobacter_jejuni Campylobacter jejuni]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LDV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LDV 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]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=OCT:N-OCTANE'>OCT</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=5ldv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ldv OCA], [https://pdbe.org/5ldv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ldv RCSB], [https://www.ebi.ac.uk/pdbsum/5ldv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ldv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q659I5_CAMJU Q659I5_CAMJU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Gram-negative organism Campylobacter jejuni is the major cause of food poisoning. Unlike Escherichia coli, which has two major porins, OmpC and OmpF, C. jejuni has one, termed major outer membrane protein (MOMP) through which nutrients and antibiotics transit. We report the 2.1-A crystal structure of C. jejuni MOMP expressed in E. coli and a lower resolution but otherwise identical structure purified directly from C. jejuni. The 2.1-A resolution structure of recombinant MOMP showed that although the protein has timeric arrangement similar to OmpC, it is an 18-stranded, not 16-stranded, beta-barrel. The structure has identified a Ca2+ bound at the constriction zone, which is functionally significant as suggested by molecular dynamics and single-channel experiments. The water-filled channel of MOMP has a narrow constriction zone, and single-molecule studies show a monomeric conductivity of 0.7+/-0.2 nS and a trimeric conductance of 2.2+/-0.2 nS. The ion neutralizes negative charges at the constriction zone, reducing the transverse electric field and reversing ion selectivity. Modeling of the transit of ciprofloxacin, an antibiotic of choice for treating Campylobacter infection, through the pore of MOMP reveals a trajectory that is dependent upon the presence metal ion.

MOMP from Campylobacter jejuni Is a Trimer of 18-Stranded beta-Barrel Monomers with a Ca2+ Ion Bound at the Constriction Zone.,Ferrara LG, Wallat GD, Moynie L, Dhanasekar NN, Aliouane S, Acosta-Gutierrez S, Pages JM, Bolla JM, Winterhalter M, Ceccarelli M, Naismith JH J Mol Biol. 2016 Sep 30. pii: S0022-2836(16)30401-6. doi:, 10.1016/j.jmb.2016.09.021. PMID:27693650<ref>PMID:27693650</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5ldv" style="background-color:#fffaf0;"></div>

==See Also==
*[[Porin 3D structures|Porin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Campylobacter jejuni]]
[[Category: Large Structures]]
[[Category: Ferrara LMG]]
[[Category: Moynie L]]
[[Category: Naismith JH]]
[[Category: Wallat GD]]