View source for 5hsp


==MamM CTD M250L==
<StructureSection load='5hsp' size='340' side='right'caption='[[5hsp]], [[Resolution|resolution]] 1.79&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5hsp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Magnetospirillum_gryphiswaldense Magnetospirillum gryphiswaldense]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HSP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HSP 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]] 1.79&#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=5hsp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hsp OCA], [https://pdbe.org/5hsp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hsp RCSB], [https://www.ebi.ac.uk/pdbsum/5hsp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hsp 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 highly conserved, metal ion efflux transporters that maintain divalent transition metal cation homeostasis. Most CDF proteins contain two domains, the cation transporting transmembrane domain and the regulatory cytoplasmic C-terminal domain (CTD). MamM is a magnetosome-associated CDF protein essential for the biomineralization of magnetic iron-oxide particles in magnetotactic bacteria. To investigate the structure-function relationship of CDF cytoplasmic domains, we characterized a MamM M250P mutation that is synonymous with the disease-related mutation L349P of the human CDF protein ZnT-10. Our results show that the M250P exchange in MamM causes severe structural changes in its CTD resulting in abnormal reduced function. Our in vivo, in vitro and in silico studies indicate that the CTD fold is critical for CDF proteins' proper function and support the previously suggested role of the CDF cytoplasmic domain as a CDF regulatory element. Based on our results, we also suggest a mechanism for the effects of the ZnT-10 L349P mutation in human.

Disease-Homologous Mutation in the Cation Diffusion Facilitator Protein MamM Causes Single-Domain Structural Loss and Signifies Its Importance.,Barber-Zucker S, Uebe R, Davidov G, Navon Y, Sherf D, Chill JH, Kass I, Bitton R, Schuler D, Zarivach R Sci Rep. 2016 Aug 23;6:31933. doi: 10.1038/srep31933. PMID:27550551<ref>PMID:27550551</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5hsp" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Magnetospirillum gryphiswaldense]]
[[Category: Barber-Zucker S]]
[[Category: Zarivach R]]