Crystal structure of BamB bound to a periplasmic domain fragment of BamA, the central component of the β-barrel assembly machine.

The β-barrel assembly machinery (BAM) mediates folding and insertion of β-barrel outer membrane proteins (OMPs) into the outer membrane of Gram-negative bacteria. BAM is a five-protein complex consisting of the β-barrel OMP BamA and lipoproteins BamB, -C, -D, and -E. High resolution structures of all the individual BAM subunits and a BamD-BamC complex have been determined.

Short cervix and vaginal progesterone: a model on how to tackle the problem of idiopathic preterm labor.

Preterm deliveries continue to be a major problem in obstetrics and pediatrics. Short cervical length has been identified as the most accurate way to predict preterm delivery. Recently, vaginally administered progesterone has been shown in separate studies to dramatically decrease the prematurity rate in patients with a short cervix.

Crystal structure of BamB from Pseudomonas aeruginosa and functional evaluation of its conserved structural features.

The assembly of β-barrel Outer Membrane Proteins (OMPs) in the outer membrane is essential for gram-negative bacteria. The process requires the β-Barrel Assembly Machine (BAM), a multiprotein complex that, in E. coli, is composed of the OMP BamA and four lipoproteins BamB-E.

Structure of the BamC two-domain protein obtained by Rosetta with a limited NMR data set.

The CS-RDC-NOE Rosetta program was used to generate the solution structure of a 27-kDa fragment of the Escherichia coli BamC protein from a limited set of NMR data. The BamC protein is a component of the essential five-protein β-barrel assembly machine in E. coli.

Crystal structure of BamD: an essential component of the β-Barrel assembly machinery of gram-negative bacteria.

Folding and insertion of integral β-barrel proteins in the outer membrane (OM) is an essential process for Gram-negative bacteria that requires the β-barrel assembly machinery (BAM). Efficient OM protein (OMP) folding and insertion appears to require a consensus C-terminal signal in OMPs characterized by terminal F or W residues. The BAM complex is embedded in the OM and, in Escherichia coli, consists of the β-barrel BamA and four lipoproteins BamBCDE.