5i69 | pdb_00005i69
MBP-MamC magnetite-interaction component mutant-D70A
Structural highlights
FunctionMALE_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 PubMedMagnetotactic 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
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