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3W8G

MamM V260R

Summary for 3W8G
Entry DOI10.2210/pdb3w8g/pdb
Related3W5X 3W5Y 3W5Z 3W60 3W61 3W62 3W63 3W64 3W65 3W66
DescriptorMagnetosome protein MamM (2 entities in total)
Functional Keywordscation diffusion facilitator (cdf), metal ion transport, metal transport
Biological sourceMagnetospirillum gryphiswaldense
Total number of polymer chains2
Total formula weight23936.92
Authors
Zeytuni, N.,Davidov, G.,Zarivach, R. (deposition date: 2013-03-12, release date: 2014-06-11, Last modification date: 2023-11-08)
Primary citationZeytuni, 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, 9:e97154-e97154, 2014
Cited by
PubMed Abstract: 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.
PubMed: 24819161
DOI: 10.1371/journal.pone.0097154
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.05 Å)
Structure validation

227111

數據於2024-11-06公開中

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