View source for 3w66


==MamM-CTD D249A and H285A==
<StructureSection load='3w66' size='340' side='right'caption='[[3w66]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3w66]] is a 1 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=3W66 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3W66 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]] 2.05&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</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=3w66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w66 OCA], [https://pdbe.org/3w66 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w66 RCSB], [https://www.ebi.ac.uk/pdbsum/3w66 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w66 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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3w66" 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]]