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, 81 (1), pp. 56-68, 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 ?? 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 |
| Export: | |
| Suche nach Titel in: | TUfind oder in Google |
 |
Send an inquiry |
Options (only for editors)
 |
View Item |
Drucken
Impressum