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3w8g

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MamM V260R

Structural highlights

3w8g is a 2 chain structure with sequence from Magnetospirillum gryphiswaldense MSR-1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.05Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MAMM_MAGGM Essential for magnetosome formation; required for stable accumulation of MamB (PubMed:22007638). May nucleate iron crystal formation (Probable). Probably binds and transports iron. Binds divalent cations, possibly up to 3 Zn(2+) per dimer in vitro, probably iron in vivo (Probable) (PubMed:30811856). One of 7 genes (mamLQBIEMO) able to induce magnetosome membrane biogenesis; coexpression of mamLQRBIEMO in a deletion of the 17 gene mamAB operon restores magnetosome vesicle formation but not magnetite biosynthesis (PubMed:27286560).^[1] ^[2] ^[3] ^[4] ^[5] ^[6]

Publication Abstract from PubMed

Cation diffusion facilitators (CDF) are part of a highly conserved protein family that maintains cellular divalent cation homeostasis in all organisms. CDFs were found to be involved in numerous human health conditions, such as Type-II diabetes and neurodegenerative diseases. In this work, we established the magnetite biomineralizing alphaproteobacterium Magnetospirillum gryphiswaldense as an effective model system to study CDF-related Type-II diabetes. Here, we introduced two ZnT-8 Type-II diabetes-related mutations into the M. gryphiswaldense MamM protein, a magnetosome-associated CDF transporter essential for magnetite biomineralization within magnetosome vesicles. The mutations' effects on magnetite biomineralization and iron transport within magnetosome vesicles were tested in vivo. Additionally, by combining several in vitro and in silico methodologies we provide new mechanistic insights for ZnT-8 polymorphism at position 325, located at a crucial dimerization site important for CDF regulation and activation. Overall, by following differentiated, easily measurable, magnetism-related phenotypes we can utilize magnetotactic bacteria for future research of CDF-related human diseases.

Bacterial Magnetosome Biomineralization - A Novel Platform to Study Molecular Mechanisms of Human CDF-Related Type-II Diabetes.,Zeytuni N, Uebe R, Maes M, Davidov G, Baram M, Raschdorf O, Friedler A, Miller Y, Schuler D, Zarivach R PLoS One. 2014 May 12;9(5):e97154. doi: 10.1371/journal.pone.0097154. eCollection, 2014. PMID:24819161^[7]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Uebe R, Junge K, Henn V, Poxleitner G, Katzmann E, Plitzko JM, Zarivach R, Kasama T, Wanner G, Pósfai M, Böttger L, Matzanke B, Schüler D. The cation diffusion facilitator proteins MamB and MamM of Magnetospirillum gryphiswaldense have distinct and complex functions, and are involved in magnetite biomineralization and magnetosome membrane assembly. Mol Microbiol. 2011 Nov;82(4):818-35. PMID:22007638 doi:10.1111/j.1365-2958.2011.07863.x
↑ Raschdorf O, Forstner Y, Kolinko I, Uebe R, Plitzko JM, Schüler D. Genetic and Ultrastructural Analysis Reveals the Key Players and Initial Steps of Bacterial Magnetosome Membrane Biogenesis. PLoS Genet. 2016 Jun 10;12(6):e1006101. PMID:27286560 doi:10.1371/journal.pgen.1006101
↑ Barber-Zucker S, Hall J, Mangapuram SV, Kass I, Kolusheva S, MacMillan F, Zarivach R, Henn A. Metal binding to the dynamic cytoplasmic domain of the cation diffusion facilitator (CDF) protein MamM induces a 'locked-in' configuration. FEBS J. 2019 Feb 27. doi: 10.1111/febs.14795. PMID:30811856 doi:http://dx.doi.org/10.1111/febs.14795
↑ Uebe R, Junge K, Henn V, Poxleitner G, Katzmann E, Plitzko JM, Zarivach R, Kasama T, Wanner G, Pósfai M, Böttger L, Matzanke B, Schüler D. The cation diffusion facilitator proteins MamB and MamM of Magnetospirillum gryphiswaldense have distinct and complex functions, and are involved in magnetite biomineralization and magnetosome membrane assembly. Mol Microbiol. 2011 Nov;82(4):818-35. PMID:22007638 doi:10.1111/j.1365-2958.2011.07863.x
↑ Zeytuni N, Uebe R, Maes M, Davidov G, Baram M, Raschdorf O, Nadav-Tsubery M, Kolusheva S, Bitton R, Goobes G, Friedler A, Miller Y, Schuler D, Zarivach R. Cation diffusion facilitators transport initiation and regulation is mediated by cation induced conformational changes of the cytoplasmic domain. PLoS One. 2014 Mar 21;9(3):e92141. doi: 10.1371/journal.pone.0092141. eCollection, 2014. PMID:24658343 doi:http://dx.doi.org/10.1371/journal.pone.0092141
↑ Zeytuni N, Uebe R, Maes M, Davidov G, Baram M, Raschdorf O, Friedler A, Miller Y, Schuler D, Zarivach R. Bacterial Magnetosome Biomineralization - A Novel Platform to Study Molecular Mechanisms of Human CDF-Related Type-II Diabetes. PLoS One. 2014 May 12;9(5):e97154. doi: 10.1371/journal.pone.0097154. eCollection, 2014. PMID:24819161 doi:http://dx.doi.org/10.1371/journal.pone.0097154
↑ Zeytuni N, Uebe R, Maes M, Davidov G, Baram M, Raschdorf O, Friedler A, Miller Y, Schuler D, Zarivach R. Bacterial Magnetosome Biomineralization - A Novel Platform to Study Molecular Mechanisms of Human CDF-Related Type-II Diabetes. PLoS One. 2014 May 12;9(5):e97154. doi: 10.1371/journal.pone.0097154. eCollection, 2014. PMID:24819161 doi:http://dx.doi.org/10.1371/journal.pone.0097154