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| | <StructureSection load='5i69' size='340' side='right'caption='[[5i69]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='5i69' size='340' side='right'caption='[[5i69]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5i69]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5I69 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5I69 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5i69]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Magnetospirillum_magneticum_AMB-1 Magnetospirillum magneticum AMB-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5I69 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5I69 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MAL:MALTOSE'>MAL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.7Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">malE, b4034, JW3994 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5i69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i69 OCA], [http://pdbe.org/5i69 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5i69 RCSB], [http://www.ebi.ac.uk/pdbsum/5i69 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5i69 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=5i69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i69 OCA], [https://pdbe.org/5i69 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5i69 RCSB], [https://www.ebi.ac.uk/pdbsum/5i69 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5i69 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI]] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides. | + | [https://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.[https://www.uniprot.org/uniprot/MAMC_MAGSA MAMC_MAGSA] Probably involved in magnetite crystal growth (Probable). The lumenal domain may bind the magnetite crystals, affecting crystal size and shape (Probable).<ref>PMID:24961165</ref> <ref>PMID:26970040</ref> <ref>PMID:30405554</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: Ecoli]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Davidove, G]] | + | [[Category: Magnetospirillum magneticum AMB-1]] |
| - | [[Category: Faivre, D]] | + | [[Category: Davidove G]] |
| - | [[Category: Gonzalez, T P]] | + | [[Category: Faivre D]] |
| - | [[Category: Grimberg, N]] | + | [[Category: Gonzalez TP]] |
| - | [[Category: Jimenez-Lopez, C]] | + | [[Category: Grimberg N]] |
| - | [[Category: Kolusheva, S]] | + | [[Category: Jimenez-Lopez C]] |
| - | [[Category: Levi, H]] | + | [[Category: Kolusheva S]] |
| - | [[Category: Nelkenbaum, O]] | + | [[Category: Levi H]] |
| - | [[Category: Nudelman, H]] | + | [[Category: Nelkenbaum O]] |
| - | [[Category: Tercedor, C V]] | + | [[Category: Nudelman H]] |
| - | [[Category: Widdrat, M]] | + | [[Category: Tercedor CV]] |
| - | [[Category: Zarivach, R]] | + | [[Category: Widdrat M]] |
| - | [[Category: Biomineralization]]
| + | [[Category: Zarivach R]] |
| - | [[Category: Magnetite]]
| + | |
| - | [[Category: Magnetite binding protein]]
| + | |
| - | [[Category: Magnetotactic bacteria]]
| + | |
| - | [[Category: Mamc]]
| + | |
| - | [[Category: Protein-mineral interaction]]
| + | |
| Structural highlights
Function
MALE_ECOLI Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.MAMC_MAGSA Probably involved in magnetite crystal growth (Probable). The lumenal domain may bind the magnetite crystals, affecting crystal size and shape (Probable).[1] [2] [3]
Publication Abstract from PubMed
Magnetotactic bacteria are Gram-negative bacteria that navigate along geomagnetic fields using the magnetosome, an organelle that consists of a membrane-enveloped magnetic nanoparticle. Magnetite formation and its properties are controlled by a specific set of proteins. MamC is a small magnetosome-membrane protein that is known to be active in iron biomineralization but its mechanism has yet to be clarified. Here, we studied the relationship between the MamC magnetite-interaction loop (MIL) structure and its magnetite interaction using an inert biomineralization protein-MamC chimera. Our determined structure shows an alpha-helical fold for MamC-MIL with highly charged surfaces. Additionally, the MamC-MIL induces the formation of larger magnetite crystals compared to protein-free and inert biomineralization protein control experiments. We suggest that the connection between the MamC-MIL structure and the protein's charged surfaces is crucial for magnetite binding and thus for the size control of the magnetite nanoparticles.
Structure-function studies of the magnetite-biomineralizing magnetosome-associated protein MamC.,Nudelman H, Valverde-Tercedor C, Kolusheva S, Perez Gonzalez T, Widdrat M, Grimberg N, Levi H, Nelkenbaum O, Davidov G, Faivre D, Jimenez-Lopez C, Zarivach R J Struct Biol. 2016 Jun;194(3):244-52. doi: 10.1016/j.jsb.2016.03.001. Epub 2016 , Mar 10. PMID:26970040[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Arakaki A, Yamagishi A, Fukuyo A, Tanaka M, Matsunaga T. Co-ordinated functions of Mms proteins define the surface structure of cubo-octahedral magnetite crystals in magnetotactic bacteria. Mol Microbiol. 2014 Aug;93(3):554-67. PMID:24961165 doi:10.1111/mmi.12683
- ↑ Nudelman H, Valverde-Tercedor C, Kolusheva S, Perez Gonzalez T, Widdrat M, Grimberg N, Levi H, Nelkenbaum O, Davidov G, Faivre D, Jimenez-Lopez C, Zarivach R. Structure-function studies of the magnetite-biomineralizing magnetosome-associated protein MamC. J Struct Biol. 2016 Jun;194(3):244-52. doi: 10.1016/j.jsb.2016.03.001. Epub 2016 , Mar 10. PMID:26970040 doi:http://dx.doi.org/10.1016/j.jsb.2016.03.001
- ↑ Nudelman H, Lee YZ, Hung YL, Kolusheva S, Upcher A, Chen YC, Chen JY, Sue SC, Zarivach R. Understanding the Biomineralization Role of Magnetite-Interacting Components (MICs) From Magnetotactic Bacteria. Front Microbiol. 2018 Oct 23;9:2480. PMID:30405554 doi:10.3389/fmicb.2018.02480
- ↑ Nudelman H, Valverde-Tercedor C, Kolusheva S, Perez Gonzalez T, Widdrat M, Grimberg N, Levi H, Nelkenbaum O, Davidov G, Faivre D, Jimenez-Lopez C, Zarivach R. Structure-function studies of the magnetite-biomineralizing magnetosome-associated protein MamC. J Struct Biol. 2016 Jun;194(3):244-52. doi: 10.1016/j.jsb.2016.03.001. Epub 2016 , Mar 10. PMID:26970040 doi:http://dx.doi.org/10.1016/j.jsb.2016.03.001
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