5fvn | pdb_00005fvn

X-ray crystal structure of Enterobacter cloacae OmpE36 porin.

spinqualitylabelsall models 5fvn, resolution 1.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5fvn is a 6 chain structure with sequence from Enterobacter cloacae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: C8E, CA, DAO, FTT, GMH, GP1, KDO, MYR, PO4, SO4, Z9M Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q93K99_ENTCL 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. Gram-negative trimeric porins have specific LPS binding sites that are essential for porin biogenesis.,Arunmanee W, Pathania M, Solovyova AS, Le Brun AP, Ridley H, Basle A, van den Berg B, Lakey JH Proc Natl Acad Sci U S A. 2016 Aug 23;113(34):E5034-43. doi:, 10.1073/pnas.1602382113. Epub 2016 Aug 4. PMID:27493217 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Porin 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA