@article{Albrecht2014Struc-29871,
  year={2014},
  doi={10.1107/S1399004714007482},
  title={Structure of BamA, an essential factor in outer membrane protein biogenesis},
  number={6},
  volume={70},
  issn={0907-4449},
  journal={Acta Crystallographica Section D : Biological Crystallography},
  pages={1779--1789},
  author={Albrecht, Reinhard and Schütz, Monika and Oberhettinger, Philipp and Faulstich, Michaela and Bermejo, Ivan and Rudel, Thomas and Diederichs, Kay and Zeth, Kornelius}
}

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    <dc:creator>Albrecht, Reinhard</dc:creator>
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    <dc:creator>Schütz, Monika</dc:creator>
    <dc:creator>Bermejo, Ivan</dc:creator>
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    <dc:contributor>Bermejo, Ivan</dc:contributor>
    <dcterms:title>Structure of BamA, an essential factor in outer membrane protein biogenesis</dcterms:title>
    <dc:contributor>Albrecht, Reinhard</dc:contributor>
    <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/29871"/>
    <dc:rights>terms-of-use</dc:rights>
    <dc:contributor>Schütz, Monika</dc:contributor>
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    <dc:creator>Oberhettinger, Philipp</dc:creator>
    <dc:creator>Rudel, Thomas</dc:creator>
    <dc:creator>Diederichs, Kay</dc:creator>
    <dc:contributor>Diederichs, Kay</dc:contributor>
    <dcterms:abstract xml:lang="eng">Outer membrane protein (OMP) biogenesis is an essential process for maintaining the bacterial cell envelope and involves the β-barrel assembly machinery (BAM) for OMP recognition, folding and assembly. In Escherichia coli this function is orchestrated by five proteins: the integral outer membrane protein BamA of the Omp85 superfamily and four associated lipoproteins. To unravel the mechanism underlying OMP folding and insertion, the structure of the E. coli BamA β-barrel and P5 domain was determined at 3 Å resolution. These data add information beyond that provided in the recently published crystal structures of BamA from Haemophilus ducreyi and Neisseria gonorrhoeae and are a valuable basis for the interpretation of pertinent functional studies. In an `open' conformation, E. coli BamA displays a significant degree of flexibility between P5 and the barrel domain, which is indicative of a multi-state function in substrate transfer. E. coli BamA is characterized by a discontinuous β-barrel with impaired β1–β16 strand interactions denoted by only two connecting hydrogen bonds and a disordered C-terminus. The 16-stranded barrel surrounds a large cavity which implies a function in OMP substrate binding and partial folding. These findings strongly support a mechanism of OMP biogenesis in which substrates are partially folded inside the barrel cavity and are subsequently released laterally into the lipid bilayer.</dcterms:abstract>
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    <dc:contributor>Oberhettinger, Philipp</dc:contributor>
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    <dc:creator>Zeth, Kornelius</dc:creator>
    <dc:contributor>Zeth, Kornelius</dc:contributor>
    <dc:contributor>Faulstich, Michaela</dc:contributor>
    <dc:language>eng</dc:language>
    <dc:creator>Faulstich, Michaela</dc:creator>
    <dc:contributor>Rudel, Thomas</dc:contributor>
    <dcterms:issued>2014</dcterms:issued>
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