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Crystallizing the function of the magnetosome membrane mineralization protein Mms6
The literature on the magnetosome membrane (MM) protein, magnetosome membrane specific6 (Mms6), is reviewed. Mms6 is native to magnetotactic bacteria (MTB). These bacteria take up iron from solution and biomineralize magnetite nanoparticles within organelles called magnetosomes. Mms6 is a small prot...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Portland Press Ltd.
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4900750/ https://www.ncbi.nlm.nih.gov/pubmed/27284056 http://dx.doi.org/10.1042/BST20160057 |
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author | Staniland, Sarah S. Rawlings, Andrea E. |
author_facet | Staniland, Sarah S. Rawlings, Andrea E. |
author_sort | Staniland, Sarah S. |
collection | PubMed |
description | The literature on the magnetosome membrane (MM) protein, magnetosome membrane specific6 (Mms6), is reviewed. Mms6 is native to magnetotactic bacteria (MTB). These bacteria take up iron from solution and biomineralize magnetite nanoparticles within organelles called magnetosomes. Mms6 is a small protein embedded on the interior of the MM and was discovered tightly associated with the formed mineral. It has been the subject of intensive research as it is seen to control the formation of particles both in vivo and in vitro. Here, we compile, review and discuss the research detailing Mms6’s activity within the cell and in a range of chemical in vitro methods where Mms6 has a marked effect on the composition, size and distribution of synthetic particles, with approximately 21 nm in size for solution precipitations and approximately 90 nm for those formed on surfaces. Furthermore, we review and discuss recent work detailing the structure and function of Mms6. From the evidence, we propose a mechanism for its function as a specific magnetite nucleation protein and summaries the key features for this action: namely, self-assembly to display a charged surface for specific iron binding, with the curvature of the surfaces determining the particle size. We suggest these may aid design of biomimetic additives for future green nanoparticle production. |
format | Online Article Text |
id | pubmed-4900750 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Portland Press Ltd. |
record_format | MEDLINE/PubMed |
spelling | pubmed-49007502016-06-23 Crystallizing the function of the magnetosome membrane mineralization protein Mms6 Staniland, Sarah S. Rawlings, Andrea E. Biochem Soc Trans Biochemical Society Focused Meetings The literature on the magnetosome membrane (MM) protein, magnetosome membrane specific6 (Mms6), is reviewed. Mms6 is native to magnetotactic bacteria (MTB). These bacteria take up iron from solution and biomineralize magnetite nanoparticles within organelles called magnetosomes. Mms6 is a small protein embedded on the interior of the MM and was discovered tightly associated with the formed mineral. It has been the subject of intensive research as it is seen to control the formation of particles both in vivo and in vitro. Here, we compile, review and discuss the research detailing Mms6’s activity within the cell and in a range of chemical in vitro methods where Mms6 has a marked effect on the composition, size and distribution of synthetic particles, with approximately 21 nm in size for solution precipitations and approximately 90 nm for those formed on surfaces. Furthermore, we review and discuss recent work detailing the structure and function of Mms6. From the evidence, we propose a mechanism for its function as a specific magnetite nucleation protein and summaries the key features for this action: namely, self-assembly to display a charged surface for specific iron binding, with the curvature of the surfaces determining the particle size. We suggest these may aid design of biomimetic additives for future green nanoparticle production. Portland Press Ltd. 2016-06-09 2016-06-15 /pmc/articles/PMC4900750/ /pubmed/27284056 http://dx.doi.org/10.1042/BST20160057 Text en © 2016 The Author(s) http://creativecommons.org/licenses/by/4.0/ This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution Licence 4.0 (CC BY) (http://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Biochemical Society Focused Meetings Staniland, Sarah S. Rawlings, Andrea E. Crystallizing the function of the magnetosome membrane mineralization protein Mms6 |
title | Crystallizing the function of the magnetosome membrane mineralization protein Mms6 |
title_full | Crystallizing the function of the magnetosome membrane mineralization protein Mms6 |
title_fullStr | Crystallizing the function of the magnetosome membrane mineralization protein Mms6 |
title_full_unstemmed | Crystallizing the function of the magnetosome membrane mineralization protein Mms6 |
title_short | Crystallizing the function of the magnetosome membrane mineralization protein Mms6 |
title_sort | crystallizing the function of the magnetosome membrane mineralization protein mms6 |
topic | Biochemical Society Focused Meetings |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4900750/ https://www.ncbi.nlm.nih.gov/pubmed/27284056 http://dx.doi.org/10.1042/BST20160057 |
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