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http://purl.uniprot.org/citations/21542854http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21542854http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21542854http://www.w3.org/2000/01/rdf-schema#comment"Gas vesicles are gas-filled protein structures increasing the buoyancy of cells. The gas vesicle envelope is mainly constituted by the 8 kDa protein GvpA forming a wall with a water excluding inner surface. A structure of GvpA is not available; recent solid-state NMR results suggest a coil-α-β-β-α-coil fold. We obtained a first structural model of GvpA by high-performance de novo modelling. Attenuated total reflection (ATR)-Fourier transform infrared spectroscopy (FTIR) supported this structure. A dimer of GvpA was derived that could explain the formation of the protein monolayer in the gas vesicle wall. The hydrophobic inner surface is mainly constituted by anti-parallel β-strands. The proposed structure allows the pinpointing of contact sites that were mutated and tested for the ability to form gas vesicles in haloarchaea. Mutations in α-helix I and α-helix II, but also in the β-turn affected the gas vesicle formation, whereas other alterations had no effect. All mutants supported the structural features deduced from the model. The proposed GvpA dimers allow the formation of a monolayer protein wall, also consistent with protease treatments of isolated gas vesicles."xsd:string
http://purl.uniprot.org/citations/21542854http://purl.org/dc/terms/identifier"doi:10.1111/j.1365-2958.2011.07669.x"xsd:string
http://purl.uniprot.org/citations/21542854http://purl.org/dc/terms/identifier"doi:10.1111/j.1365-2958.2011.07669.x"xsd:string
http://purl.uniprot.org/citations/21542854http://purl.uniprot.org/core/author"Engelhardt H."xsd:string
http://purl.uniprot.org/citations/21542854http://purl.uniprot.org/core/author"Engelhardt H."xsd:string
http://purl.uniprot.org/citations/21542854http://purl.uniprot.org/core/author"Pfeifer F."xsd:string
http://purl.uniprot.org/citations/21542854http://purl.uniprot.org/core/author"Pfeifer F."xsd:string
http://purl.uniprot.org/citations/21542854http://purl.uniprot.org/core/author"Faist K."xsd:string
http://purl.uniprot.org/citations/21542854http://purl.uniprot.org/core/author"Faist K."xsd:string
http://purl.uniprot.org/citations/21542854http://purl.uniprot.org/core/author"Hamacher K."xsd:string
http://purl.uniprot.org/citations/21542854http://purl.uniprot.org/core/author"Hamacher K."xsd:string
http://purl.uniprot.org/citations/21542854http://purl.uniprot.org/core/author"Hoffgaard F."xsd:string
http://purl.uniprot.org/citations/21542854http://purl.uniprot.org/core/author"Hoffgaard F."xsd:string
http://purl.uniprot.org/citations/21542854http://purl.uniprot.org/core/author"Strunk T."xsd:string
http://purl.uniprot.org/citations/21542854http://purl.uniprot.org/core/author"Strunk T."xsd:string
http://purl.uniprot.org/citations/21542854http://purl.uniprot.org/core/author"Wenzel W."xsd:string
http://purl.uniprot.org/citations/21542854http://purl.uniprot.org/core/author"Wenzel W."xsd:string
http://purl.uniprot.org/citations/21542854http://purl.uniprot.org/core/author"Zillig M.D."xsd:string
http://purl.uniprot.org/citations/21542854http://purl.uniprot.org/core/author"Zillig M.D."xsd:string
http://purl.uniprot.org/citations/21542854http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21542854http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21542854http://purl.uniprot.org/core/name"Mol. Microbiol."xsd:string
http://purl.uniprot.org/citations/21542854http://purl.uniprot.org/core/name"Mol. Microbiol."xsd:string