@article{198996,
  keywords = {Hydrophobic and Hydrophilic Interactions, Models, Molecular, Protein Conformation, Crystallography, X-Ray, Protein Structure, Tertiary, Mutation, Escherichia coli, Molecular Sequence Data, Models, Biological, Protein Binding, Dimerization, Amino Acid Sequence, Escherichia coli Proteins, Cell Membrane, Protein Folding, Protein Structure, Secondary, Lipoproteins, Protein Transport, Bacterial Outer Membrane Proteins, Hydrogen Bonding},
  author = {Seokhee Kim and Juliana Malinverni and Piotr Sliz and Thomas Silhavy and Stephen Harrison and Daniel Kahne},
  title = {Structure and function of an essential component of the outer membrane protein assembly machine},
  abstract = {<p>Integral beta-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 beta-barrel protein precursors. Analysis of POTRA domain deletions shows which are essential and provides a view of the spatial organization of this assembly machine.</p>
},
  year = {2007},
  journal = {Science},
  volume = {317},
  pages = {961-4},
  month = {08/2007},
  issn = {1095-9203},
  doi = {10.1126/science.1143993},
  language = {eng},
}