High resolution crystal structures and molecular dynamics studies reveal substrate binding in the porin Omp32.

Crystal structure of Omp32, the anion-selective porin from Comamonas acidovorans, in complex with a periplasmic peptide at 2.1 A resolution.

BACKGROUND Porins provide diffusion channels for salts and small organic molecules in the outer membrane of bacteria. In OmpF from Escherichia coli and related porins, an electrostatic field across the channel and a potential, originating from a surplus of negative charges, create moderate cation selectivity. Here, we investigate the strongly anion-selective porin Omp32 from Comamonas acidovora...

Crystallization and preliminary X-ray crystallographic studies of the native and chemically modified anion-selective porin from Comamonas acidovorans.

Omp32, the strongly anion-selective porin from Comamonas acidovorans, has been crystallized. Two crystal forms were observed, both of which belong to space group R3, but exhibit different cell dimensions a = b = 106.7, c = 140.6 A (crystal form I) and a = b = 87.1, c = 135.3 A (crystal form II) with one trimer per asymmetric unit. The crystals diffract to 2.2 and 2.3 A resolution, respectively....

Two high-resolution crystal structures of potato 1,3-β-glucanase reveal subdomain flexibility with implications for substrate binding

Molecular dynamics simulation and docking studies on the binding properties of several anticancer drugs to human serum albumin

Disposition and transportation of anticancer drugs by human serum albumin (HSA) affects their bioavailability, distribution and elimination. In this study, the interaction of a set of anticancer drugs with HSA was investigated by molecular dynamics and molecular docking simulations. The drugs' activities were analyzed according to their docking scores, binding sites and structural descriptors. ...

Title: Gram-negative trimeric porins have specific LPS binding sites that are essential for porin biogenesis. Short title : LPS-Porin Structure

The outer membrane (OM) of Gram-negative bacteria is an unusual asymmetric bilayer with an external monolayer of lipopolysaccharide (LPS) and inner layer of phospholipids. The LPS layer is rigid and stabilized by divalent cation crosslinks between phosphate groups on the core oligosaccharide regions. This means that the OM is robust and highly impermeable to toxins and antibiotics. During their...