Structure of BamA, an essential factor in outer membrane protein biogenesis

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ALBRECHT, Reinhard, Monika SCHÜTZ, Philipp OBERHETTINGER, Michaela FAULSTICH, Ivan BERMEJO, Thomas RUDEL, Kay DIEDERICHS, Kornelius ZETH, 2014. Structure of BamA, an essential factor in outer membrane protein biogenesis. In: Acta Crystallographica Section D : Biological Crystallography. 70(6), pp. 1779-1789. ISSN 0907-4449. eISSN 1399-0047

@article{Albrecht2014Struc-29871, title={Structure of BamA, an essential factor in outer membrane protein biogenesis}, year={2014}, doi={10.1107/S1399004714007482}, 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} }

<rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/29871"> <dc:creator>Diederichs, Kay</dc:creator> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/29871"/> <dc:contributor>Albrecht, Reinhard</dc:contributor> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2015-02-18T20:08:16Z</dcterms:available> <dcterms:rights rdf:resource="http://nbn-resolving.de/urn:nbn:de:bsz:352-20150305140228786-3747162-5"/> <dc:language>eng</dc:language> <dc:creator>Oberhettinger, Philipp</dc:creator> <dcterms:issued>2014</dcterms:issued> <dcterms:title>Structure of BamA, an essential factor in outer membrane protein biogenesis</dcterms:title> <dc:creator>Schütz, Monika</dc:creator> <dc:contributor>Oberhettinger, Philipp</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> <dc:contributor>Bermejo, Ivan</dc:contributor> <dc:contributor>Zeth, Kornelius</dc:contributor> <dc:creator>Zeth, Kornelius</dc:creator> <dc:contributor>Diederichs, Kay</dc:contributor> <dc:creator>Bermejo, Ivan</dc:creator> <dc:contributor>Schütz, Monika</dc:contributor> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2015-02-18T20:08:16Z</dc:date> <dc:creator>Faulstich, Michaela</dc:creator> <dc:creator>Albrecht, Reinhard</dc:creator> <dc:creator>Rudel, Thomas</dc:creator> <dc:contributor>Rudel, Thomas</dc:contributor> <dc:contributor>Faulstich, Michaela</dc:contributor> </rdf:Description> </rdf:RDF>

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