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.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Amino Acid Sequence
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Bacterial Outer Membrane Proteins / chemistry*
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Bacterial Outer Membrane Proteins / genetics
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Bacterial Outer Membrane Proteins / metabolism*
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Cell Membrane / metabolism
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Crystallography, X-Ray
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Dimerization
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Escherichia coli / chemistry*
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Escherichia coli / metabolism*
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Escherichia coli Proteins / chemistry*
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Escherichia coli Proteins / genetics
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Escherichia coli Proteins / metabolism*
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Hydrogen Bonding
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Hydrophobic and Hydrophilic Interactions
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Lipoproteins / chemistry
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Lipoproteins / metabolism
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Models, Biological
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Models, Molecular
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Molecular Sequence Data
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Mutation
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Protein Binding
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Protein Conformation
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Protein Folding
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Protein Transport
Substances
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Bacterial Outer Membrane Proteins
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BamA protein, E coli
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Escherichia coli Proteins
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Lipoproteins
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YfgL protein, E coli