5fvn

==X-ray crystal structure of Enterobacter cloacae OmpE36 porin==

<StructureSection load='5fvn' size='340' side='right' caption='[[5fvn]], [[Resolution|resolution]] 1.45&Aring;' scene=''>

<table><tr><td colspan='2'>[[5fvn]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/"aerobacter_cloacae"_(jordan_1890)_bergey_et_al._1923 "aerobacter cloacae" (jordan 1890) bergey et al. 1923]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FVN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FVN FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DAO:LAURIC+ACID'>DAO</scene>, <scene name='pdbligand=FTT:3-HYDROXY-TETRADECANOIC+ACID'>FTT</scene>, <scene name='pdbligand=GMH:L-GLYCERO-D-MANNO-HEPTOPYRANOSE'>GMH</scene>, <scene name='pdbligand=KDO:3-DEOXY-D-MANNO-OCT-2-ULOSONIC+ACID'>KDO</scene>, <scene name='pdbligand=L1L:[(2R,3R,4R,5S,6R)-3-AZANYL-6-(HYDROXYMETHYL)-4,5-BIS(OXIDANYL)OXAN-2-YL]+DIHYDROGEN+PHOSPHATE'>L1L</scene>, <scene name='pdbligand=MYR:MYRISTIC+ACID'>MYR</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=Z9M:2-AMINO-2-DEOXY-4-O-PHOSPHONO-BETA-D-GLUCOPYRANOSE'>Z9M</scene></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5fvn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fvn OCA], [http://pdbe.org/5fvn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fvn RCSB], [http://www.ebi.ac.uk/pdbsum/5fvn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fvn ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

The outer membrane (OM) of gram-negative bacteria is an unusual asymmetric bilayer with an external monolayer of lipopolysaccharide (LPS) and an inner layer of phospholipids. The LPS layer is rigid and stabilized by divalent cation cross-links between phosphate groups on the core oligosaccharide regions. This means that the OM is robust and highly impermeable to toxins and antibiotics. During their biogenesis, OM proteins (OMPs), which function as transporters and receptors, must integrate into this ordered monolayer while preserving its impermeability. Here we reveal the specific interactions between the trimeric porins of Enterobacteriaceae and LPS. Isolated porins form complexes with variable numbers of LPS molecules, which are stabilized by calcium ions. In earlier studies, two high-affinity sites were predicted to contain groups of positively charged side chains. Mutation of these residues led to the loss of LPS binding and, in one site, also prevented trimerization of the porin, explaining the previously observed effect of LPS mutants on porin folding. The high-resolution X-ray crystal structure of a trimeric porin-LPS complex not only helps to explain the mutagenesis results but also reveals more complex, subtle porin-LPS interactions and a bridging calcium ion.

 

== References ==

[[Category: Arunmanee, W]]

[[Category: Basle, A]]

[[Category: Berg, B van den]]

[[Category: Brun, A]]

[[Category: Lakey, J H]]

[[Category: Pathania, M]]

[[Category: Ridley, H]]

[[Category: Soloyova, A]]

[[Category: Channel]]

[[Category: Trimer]]