5FVN

X-ray crystal structure of Enterobacter cloacae OmpE36 porin.

5FVN の概要

• エントリーDOI: 10.2210/pdb5fvn/pdb
• 分子名称: OMPC PORIN, MYRISTIC ACID, LAURIC ACID, ... (13 entities in total)
• 機能のキーワード: membrane protein, porin, outer membrane protein, channel, lps, trimer
• 由来する生物種: ENTEROBACTER CLOACAE
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 262359.49

構造登録者

Arunmanee, W.,Pathania, M.,Soloyova, A.,Brun, A.,Ridley, H.,Basle, A.,van den Berg, B.,Lakey, J.H. (登録日: 2016-02-09, 公開日: 2016-08-10, 最終更新日: 2024-02-07)

主引用文献

Arunmanee, W.,Pathania, M.,Solovyova, A.S.,Le Brun, A.P.,Ridley, H.,Basle, A.,van den Berg, B.,Lakey, J.H.
Gram-negative trimeric porins have specific LPS binding sites that are essential for porin biogenesis.
Proc. Natl. Acad. Sci. U.S.A., 113:E5034-E5043, 2016

PubMed Abstract: 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.

PubMed: 27493217
DOI: 10.1073/pnas.1602382113

実験手法

X-RAY DIFFRACTION (1.45 Å)