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

Strunk, Timo ; Hamacher, Kay ; Hoffgaard, Franziska ; Engelhardt, Harald ; Zillig, Martina Daniela ; Faist, Karin ; Wenzel, Wolfgang ; Pfeifer, Felicitas (2011)
Structural Model of the Gas Vesicle Protein GvpA and Analysis of GvpA Mutants in vivo.
In: Molecular microbiology, 81 (1)
Article, Bibliographie

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 ; Hamacher, Kay ; Hoffgaard, Franziska ; Engelhardt, Harald ; Zillig, Martina Daniela ; Faist, Karin ; Wenzel, Wolfgang ; Pfeifer, Felicitas
Type of entry: Bibliographie
Title: Structural Model of the Gas Vesicle Protein GvpA and Analysis of GvpA Mutants in vivo.
Language: English
Date: 2011
Journal or Publication Title: Molecular microbiology
Volume of the journal: 81
Issue Number: 1
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.

Uncontrolled Keywords: Bioinformatik
Divisions: 10 Department of Biology
?? fb10_mikrobiologie ??
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
Last Modified: 30 Apr 2018 10:46
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