Solid-state NMR evidence for inequivalent GvpA subunits in gas vesicles
Gas vesicles are organelles that provide buoyancy to the aquatic microorganisms that harbor them. The gas vesicle shell consists almost exclusively of the hydrophobic 70-residue gas vesicle protein A, arranged in an ordered array. Solid-state NMR spectra of intact collapsed gas vesicles from the cya...
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| Format: | Article |
| Language: | en_US |
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Elsevier
2012
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| Online Access: | http://hdl.handle.net/1721.1/74572 https://orcid.org/0000-0003-1589-832X |
| _version_ | 1826208911587278848 |
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| author | Sivertsen, Astrid C. Bayro, Marvin J. Belenky, Marina Griffin, Robert Guy Herzfeld, Judith |
| author2 | Massachusetts Institute of Technology. Department of Chemistry |
| author_facet | Massachusetts Institute of Technology. Department of Chemistry Sivertsen, Astrid C. Bayro, Marvin J. Belenky, Marina Griffin, Robert Guy Herzfeld, Judith |
| author_sort | Sivertsen, Astrid C. |
| collection | MIT |
| description | Gas vesicles are organelles that provide buoyancy to the aquatic microorganisms that harbor them. The gas vesicle shell consists almost exclusively of the hydrophobic 70-residue gas vesicle protein A, arranged in an ordered array. Solid-state NMR spectra of intact collapsed gas vesicles from the cyanobacterium Anabaena flos-aquae show duplication of certain gas vesicle protein A resonances, indicating that specific sites experience at least two different local environments. Interpretation of these results in terms of an asymmetric dimer repeat unit can reconcile otherwise conflicting features of the primary, secondary, tertiary, and quaternary structures of the gas vesicle protein. In particular, the asymmetric dimer can explain how the hydrogen bonds in the β-sheet portion of the molecule can be oriented optimally for strength while promoting stabilizing aromatic and electrostatic side-chain interactions among highly conserved residues and creating a large hydrophobic surface suitable for preventing water condensation inside the vesicle. |
| first_indexed | 2024-09-23T14:14:15Z |
| format | Article |
| id | mit-1721.1/74572 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T14:14:15Z |
| publishDate | 2012 |
| publisher | Elsevier |
| record_format | dspace |
| spelling | mit-1721.1/745722022-10-01T19:58:48Z Solid-state NMR evidence for inequivalent GvpA subunits in gas vesicles Sivertsen, Astrid C. Bayro, Marvin J. Belenky, Marina Griffin, Robert Guy Herzfeld, Judith Massachusetts Institute of Technology. Department of Chemistry Francis Bitter Magnet Laboratory (Massachusetts Institute of Technology) Griffin, Robert Guy Sivertsen, Astrid C. Bayro, Marvin J. Griffin, Robert Guy Gas vesicles are organelles that provide buoyancy to the aquatic microorganisms that harbor them. The gas vesicle shell consists almost exclusively of the hydrophobic 70-residue gas vesicle protein A, arranged in an ordered array. Solid-state NMR spectra of intact collapsed gas vesicles from the cyanobacterium Anabaena flos-aquae show duplication of certain gas vesicle protein A resonances, indicating that specific sites experience at least two different local environments. Interpretation of these results in terms of an asymmetric dimer repeat unit can reconcile otherwise conflicting features of the primary, secondary, tertiary, and quaternary structures of the gas vesicle protein. In particular, the asymmetric dimer can explain how the hydrogen bonds in the β-sheet portion of the molecule can be oriented optimally for strength while promoting stabilizing aromatic and electrostatic side-chain interactions among highly conserved residues and creating a large hydrophobic surface suitable for preventing water condensation inside the vesicle. National Institutes of Health (U.S.) (Grant EB002175) National Institutes of Health (U.S.) (Grant EB003151) National Institutes of Health (U.S.) (Grant EB002026) 2012-11-06T16:01:42Z 2012-11-06T16:01:42Z 2009-02 2009-02 Article http://purl.org/eprint/type/JournalArticle 0022-2836 1089-8638 http://hdl.handle.net/1721.1/74572 Sivertsen, Astrid C. et al. “Solid-State NMR Evidence for Inequivalent GvpA Subunits in Gas Vesicles.” Journal of Molecular Biology 387.4 (2009): 1032–1039. https://orcid.org/0000-0003-1589-832X en_US http://dx.doi.org/10.1016/j.jmb.2009.02.015 Journal of Molecular Biology Creative Commons Attribution-Noncommercial-Share Alike 3.0 http://creativecommons.org/licenses/by-nc-sa/3.0/ application/pdf Elsevier Prof. Griffin via Erja Kajosalo |
| spellingShingle | Sivertsen, Astrid C. Bayro, Marvin J. Belenky, Marina Griffin, Robert Guy Herzfeld, Judith Solid-state NMR evidence for inequivalent GvpA subunits in gas vesicles |
| title | Solid-state NMR evidence for inequivalent GvpA subunits in gas vesicles |
| title_full | Solid-state NMR evidence for inequivalent GvpA subunits in gas vesicles |
| title_fullStr | Solid-state NMR evidence for inequivalent GvpA subunits in gas vesicles |
| title_full_unstemmed | Solid-state NMR evidence for inequivalent GvpA subunits in gas vesicles |
| title_short | Solid-state NMR evidence for inequivalent GvpA subunits in gas vesicles |
| title_sort | solid state nmr evidence for inequivalent gvpa subunits in gas vesicles |
| url | http://hdl.handle.net/1721.1/74572 https://orcid.org/0000-0003-1589-832X |
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