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| | ==MamB-CTD mutant - D247A== | | ==MamB-CTD mutant - D247A== |
| - | <StructureSection load='5hok' size='340' side='right' caption='[[5hok]], [[Resolution|resolution]] 1.70Å' scene=''> | + | <StructureSection load='5hok' size='340' side='right'caption='[[5hok]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5hok]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Magnetospira_sp._qh-2 Magnetospira sp. qh-2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HOK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HOK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5hok]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Magnetospira_sp._QH-2 Magnetospira sp. QH-2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HOK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HOK FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mamB, MGMAQ_1061 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1288970 Magnetospira sp. QH-2])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5hok FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hok OCA], [http://pdbe.org/5hok PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hok RCSB], [http://www.ebi.ac.uk/pdbsum/5hok PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hok ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5hok FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hok OCA], [https://pdbe.org/5hok PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hok RCSB], [https://www.ebi.ac.uk/pdbsum/5hok PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hok ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/MAMB_MAGSQ MAMB_MAGSQ] Plays a dual, essential role in magnetosome formation; required for magnetosome vesicle formation as well as biomineralization (By similarity). Probably binds and transports iron (Probable). Requires heterodimerization with MamM for stability (By similarity).[UniProtKB:V6F510]<ref>PMID:29243866</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Magnetospira sp. qh-2]] | + | [[Category: Large Structures]] |
| - | [[Category: Keren, N]] | + | [[Category: Magnetospira sp. QH-2]] |
| - | [[Category: Zarivach, R]] | + | [[Category: Keren N]] |
| - | [[Category: Zeytuni, N]] | + | [[Category: Zarivach R]] |
| - | [[Category: C-terminal domain]]
| + | [[Category: Zeytuni N]] |
| - | [[Category: Cation diffusion facilitator]]
| + | |
| - | [[Category: Magnetotactic bacteria]]
| + | |
| - | [[Category: Metal transport]]
| + | |
| - | [[Category: Metal-binding site]]
| + | |
| - | [[Category: Metallochaperone like domain]]
| + | |
| Structural highlights
Function
MAMB_MAGSQ Plays a dual, essential role in magnetosome formation; required for magnetosome vesicle formation as well as biomineralization (By similarity). Probably binds and transports iron (Probable). Requires heterodimerization with MamM for stability (By similarity).[UniProtKB:V6F510][1]
Publication Abstract from PubMed
Magnetospirillum gryphiswaldense MSR-1 synthesizes membrane-enclosed magnetite (Fe3 O4 ) nanoparticles, magnetosomes, for magnetotaxis. Formation of these organelles involves a complex process comprising key steps which are governed by specific magnetosome-associated proteins. MamB, a cation diffusion facilitator (CDF) family member has been implicated in magnetosome-directed iron transport. However, deletion mutagenesis studies revealed that MamB is essential for the formation of magnetosome membrane vesicles, but its precise role remains elusive. In this study, we employed a multi-disciplinary approach to define the role of MamB during magnetosome formation. Using site-directed mutagenesis complemented by structural analyses, fluorescence microscopy and cryo-electron tomography, we show that MamB is most likely an active magnetosome-directed transporter serving two distinct, yet essential functions. First, MamB initiates magnetosome vesicle formation in a transport-independent process, probably by serving as a landmark protein. Second, MamB transport activity is required for magnetite nucleation. Furthermore, by determining the crystal structure of the MamB cytosolic C-terminal domain, we also provide mechanistic insight into transport regulation. Additionally, we present evidence that magnetosome vesicle growth and chain formation are independent of magnetite nucleation and magnetic interactions respectively. Together, our data provide novel insight into the role of the key bifunctional magnetosome protein MamB, and the early steps of magnetosome formation.
The dual role of MamB in magnetosome membrane assembly and magnetite biomineralization.,Uebe R, Keren-Khadmy N, Zeytuni N, Katzmann E, Navon Y, Davidov G, Bitton R, Plitzko JM, Schuler D, Zarivach R Mol Microbiol. 2018 Feb;107(4):542-557. doi: 10.1111/mmi.13899. Epub 2018 Jan 9. PMID:29243866[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Uebe R, Keren-Khadmy N, Zeytuni N, Katzmann E, Navon Y, Davidov G, Bitton R, Plitzko JM, Schuler D, Zarivach R. The dual role of MamB in magnetosome membrane assembly and magnetite biomineralization. Mol Microbiol. 2018 Feb;107(4):542-557. doi: 10.1111/mmi.13899. Epub 2018 Jan 9. PMID:29243866 doi:http://dx.doi.org/10.1111/mmi.13899
- ↑ Uebe R, Keren-Khadmy N, Zeytuni N, Katzmann E, Navon Y, Davidov G, Bitton R, Plitzko JM, Schuler D, Zarivach R. The dual role of MamB in magnetosome membrane assembly and magnetite biomineralization. Mol Microbiol. 2018 Feb;107(4):542-557. doi: 10.1111/mmi.13899. Epub 2018 Jan 9. PMID:29243866 doi:http://dx.doi.org/10.1111/mmi.13899
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