Investigating the ferric ion binding site of magnetite biomineralisation protein Mms6
| Autor: | Andrea E. Rawlings, Alex S. Holehouse, Sarah S. Staniland, Sybilla Louise Corbett, Panah Liravi |
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| Rok vydání: | 2019 |
| Předmět: |
Biomineralization
Luminescence Statistical methods 01 natural sciences Biochemistry chemistry.chemical_compound Binding Analysis Biochemical Simulations Magnetite 0303 health sciences Minerals Multidisciplinary Chemistry Physics Electromagnetic Radiation Statistics Mineralogy Condensed Matter Physics Monte Carlo method Physical Sciences Medicine medicine.drug Research Article Chemical Elements Plasmons Biophysical Simulations Magnetotactic bacteria Science Iron Magnetosome Biophysics 010402 general chemistry 03 medical and health sciences Bacterial Proteins medicine Ferric iron binding Amino Acid Sequence Binding site Magnetospirillum Particle Physics Chemical Characterization 030304 developmental biology Binding Sites Ligand binding assay Collective Excitations Biology and Life Sciences Computational Biology Ferrosoferric Oxide 0104 chemical sciences Research and analysis methods Mutation Earth Sciences Ferric Mathematical and statistical techniques Mathematics |
| Zdroj: | PLoS ONE PLoS ONE, Vol 15, Iss 2, p e0228708 (2020) |
| ISSN: | 1932-6203 |
| Popis: | The biomineralization protein Mms6 has been shown to be a major player in the formation of magnetic nanoparticles both within the magnetosomes of magnetotactic bacteria and as an additive in synthetic magnetite precipitation assays. Previous studies have highlighted the ferric iron binding capability of the protein and this activity is thought to be crucial to its mineralizing properties. To understand how this protein binds ferric ions we have prepared a series of single amino acid substitutions within the C-terminal binding region of Mms6 and have used a ferric binding assay to probe the binding site at the level of individual residues which has pinpointed the key residues of E44, E50 and R55 involved in Mms6 ferric binding. No aspartic residues bound ferric ions. A nanoplasmonic sensing experiment was used to investigate the unstable EER44, 50,55AAA triple mutant in comparison to native Mms6. This suggests a difference in interaction with iron ions between the two and potential changes to the surface precipitation of iron oxide when the pH is increased. All-atom simulations suggest that disruptive mutations do not fundamentally alter the conformational preferences of the ferric binding region. Instead, disruption of these residues appears to impede a sequence-specific motif in the C-terminus critical to ferric ion binding. |
| Databáze: | OpenAIRE |
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