Conserved residues of the putative L6 loop of Escherichia coli BamA play a critical role in the assembly of β-barrel outer membrane proteins, including that of BamA itself.

Abstract excerpt

Many members of the Omp85 family of proteins form essential β-barrel outer membrane protein (OMP) biogenesis machinery in Gram-negative bacteria, chloroplasts, and mitochondria. In Escherichia coli, BamA, a member of the Omp85 family, folds into an outer membrane-embedded β-barrel domain and a soluble periplasmic polypeptide-transport-associated (POTRA) domain. Although the high-resolution structures of only the...

Topics

• Amino Acid Substitution
• Bacterial Outer Membrane Proteins
• Escherichia coli
• Escherichia coli Proteins
• Models, Molecular
• Phenotype
• Protein Conformation
• Protein Folding
• Protein Structure, Secondary
• Protein Structure, Tertiary