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3W63

MamM-CTD 215-293

Summary for 3W63
Entry DOI10.2210/pdb3w63/pdb
Related3W5X 3W5Y 3W5Z 3W60 3W61 3W62 3W64 3W65 3W66 3W8P
DescriptorMagnetosome protein MamM, SULFATE ION (3 entities in total)
Functional Keywordscation diffusion facilitator (cdf), divalent cation transport, metal ion transport, metal transport
Biological sourceMagnetospirillum gryphiswaldense
Total number of polymer chains1
Total formula weight9360.55
Authors
Zeytuni, N.,Davidov, G.,Zarivach, R. (deposition date: 2013-02-10, release date: 2014-04-16, Last modification date: 2023-11-08)
Primary citationZeytuni, 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, 9:e92141-e92141, 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 domains of life. CDF's were shown to be involved in several human diseases, such as Type-II diabetes and neurodegenerative diseases. In this work, we employed a multi-disciplinary approach to study the activation mechanism of the CDF protein family. For this we used MamM, one of the main ion transporters of magnetosomes--bacterial organelles that enable magnetotactic bacteria to orientate along geomagnetic fields. Our results reveal that the cytosolic domain of MamM forms a stable dimer that undergoes distinct conformational changes upon divalent cation binding. MamM conformational change is associated with three metal binding sites that were identified and characterized. Altogether, our results provide a novel auto-regulation mode of action model in which the cytosolic domain's conformational changes upon ligand binding allows the priming of the CDF into its transport mode.
PubMed: 24658343
DOI: 10.1371/journal.pone.0092141
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

226707

數據於2024-10-30公開中

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