PMID:17702946
| Citation |
Kim, S, Malinverni, JC, Sliz, P, Silhavy, TJ, Harrison, SC and Kahne, D (2007) Structure and function of an essential component of the outer membrane protein assembly machine. Science 317:961-4 |
|---|---|
| Abstract |
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. |
| Links |
PubMed Online version:10.1126/science.1143993 |
| Keywords |
Amino Acid Sequence; Bacterial Outer Membrane Proteins/chemistry; Bacterial Outer Membrane Proteins/genetics; Bacterial Outer Membrane Proteins/metabolism; Cell Membrane/metabolism; Crystallography, X-Ray; Dimerization; Escherichia coli/chemistry; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Hydrogen Bonding; Hydrophobic and Hydrophilic Interactions; Lipoproteins/chemistry; Lipoproteins/metabolism; Models, Biological; Models, Molecular; Molecular Sequence Data; Mutation; Protein Binding; Protein Conformation; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Protein Transport |
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