3w5y

From Proteopedia

(Difference between revisions)

Current revision

MamM-CTD

Structural highlights

3w5y 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 1.95Å
Ligands:
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 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.

Cation diffusion facilitators transport initiation and regulation is mediated by cation induced conformational changes of the cytoplasmic domain.,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 PLoS One. 2014 Mar 21;9(3):e92141. doi: 10.1371/journal.pone.0092141. eCollection, 2014. PMID:24658343^[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, 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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3w5y"

Categories: Large Structures | Magnetospirillum gryphiswaldense MSR-1 | Davidov G | Zarivach R | Zeytuni N

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 3w5y is ON HOLD
+==MamM-CTD==
+<StructureSection load='3w5y' size='340' side='right'caption='[[3w5y]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[3w5y]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Magnetospirillum_gryphiswaldense_MSR-1 Magnetospirillum gryphiswaldense MSR-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W5Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3W5Y FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=3w5y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w5y OCA], [https://pdbe.org/3w5y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w5y RCSB], [https://www.ebi.ac.uk/pdbsum/3w5y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w5y ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/MAMM_MAGGM 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).<ref>PMID:22007638</ref> <ref>PMID:27286560</ref> <ref>PMID:30811856</ref> <ref>PMID:22007638</ref> <ref>PMID:24658343</ref> <ref>PMID:24819161</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-Authors: Zeytuni, N., Davidov, G., Zarivach, R.
+Cation diffusion facilitators transport initiation and regulation is mediated by cation induced conformational changes of the cytoplasmic domain.,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 PLoS One. 2014 Mar 21;9(3):e92141. doi: 10.1371/journal.pone.0092141. eCollection, 2014. PMID:24658343<ref>PMID:24658343</ref>
-Description: MamM-CTD
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3w5y" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Magnetospirillum gryphiswaldense MSR-1]]
+[[Category: Davidov G]]
+[[Category: Zarivach R]]
+[[Category: Zeytuni N]]

3w5y

From Proteopedia

Current revision

MamM-CTD

Structural highlights

Function

Publication Abstract from PubMed

References

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