Structure and Function of an Essential Component of the Outer Membrane Protein Assembly Machine

• Published in: Science (American Association for the Advancement of Science) Vol. 317; no. 5840; pp. 961 - 964
• Main Authors: Kim, Seokhee, Malinverni, Juliana C, Sliz, Piotr, Silhavy, Thomas J, Harrison, Stephen C, Kahne, Daniel
• Format: Journal Article
• Language: English
• Published: Washington, DC American Association for the Advancement of Science 17.08.2007; The American Association for the Advancement of Science
• Subjects: Amino Acid Sequence; Antibodies; Bacteria; Bacterial Outer Membrane Proteins - chemistry; Bacterial Outer Membrane Proteins - genetics; Bacterial Outer Membrane Proteins - metabolism; Binding sites; Biochemistry; Biological and medical sciences; Cell Membrane - metabolism; Crystal structure; Crystalline structure; Crystallography, X-Ray; Crystals; Dimerization; Dimers; E coli; Escherichia coli - chemistry; Escherichia coli - metabolism; Escherichia coli Proteins - chemistry; Escherichia coli Proteins - genetics; Escherichia coli Proteins - metabolism; Fundamental and applied biological sciences. Psychology; Hydrogen Bonding; Hydrophobic and Hydrophilic Interactions; Lipoproteins; Lipoproteins - chemistry; Lipoproteins - metabolism; Membrane proteins; Mitochondria; Models, Biological; Models, Molecular; Molecular biophysics; Molecular Sequence Data; Monomers; Mutation; Protein Binding; Protein Conformation; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Protein Transport; Proteins; Structure in molecular biology; Bacteria; Membrane protein; External membrane; Escherichia coli; Enterobacteriaceae; Crystalline structure
• ISSN: 0036-8075; 1095-9203
• DOI: 10.1126/science.1143993

Integral β-barrel proteins are found in the outer membranes of mitochondria, chloroplasts, and Gram-negative bacteria. The machine that assembles these proteins contains an integral membrane protein, called YaeT in Escherichia coli, which has one or more polypeptide transport-associated (POTRA) domains. The crystal structure of a periplasmic fragment of YaeT reveals the POTRA domain fold and suggests a model for how POTRA domains can bind different peptide sequences, as required for a machine that handles numerous β-barrel protein precursors. Analysis of POTRA domain deletions shows which are essential and provides a view of the spatial organization of this assembly machine.