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Structural Model of the Gas Vesicle Protein GvpA and Analysis of GvpA Mutants in vivo.

Strunk, Timo and Hamacher, Kay and Hoffgaard, Franziska and Engelhardt, Harald and Zillig, Martina Daniela and Faist, Karin and Wenzel, Wolfgang and Pfeifer, Felicitas (2011):
Structural Model of the Gas Vesicle Protein GvpA and Analysis of GvpA Mutants in vivo.
In: Molecular microbiology, pp. 56-68, 81, (1), ISSN 1365-2958,
[Article]

Abstract

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 modeling. ATR-FTIR spectroscopy 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.

Item Type: Article
Erschienen: 2011
Creators: Strunk, Timo and Hamacher, Kay and Hoffgaard, Franziska and Engelhardt, Harald and Zillig, Martina Daniela and Faist, Karin and Wenzel, Wolfgang and Pfeifer, Felicitas
Title: Structural Model of the Gas Vesicle Protein GvpA and Analysis of GvpA Mutants in vivo.
Language: English
Abstract:

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 modeling. ATR-FTIR spectroscopy 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.

Journal or Publication Title: Molecular microbiology
Volume: 81
Number: 1
Uncontrolled Keywords: Bioinformatik
Divisions: 10 Department of Biology
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10 Department of Biology > Computational Biology and Simulation
10 Department of Biology > Microbiology and Archaea
20 Department of Computer Science
Date Deposited: 10 May 2011 09:02
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