View source for 3as4


==MamA AMB-1 C2221==
<StructureSection load='3as4' size='340' side='right'caption='[[3as4]], [[Resolution|resolution]] 2.33&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3as4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Magnetospirillum_magneticum_AMB-1 Magnetospirillum magneticum AMB-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AS4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AS4 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]] 2.33&#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=3as4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3as4 OCA], [https://pdbe.org/3as4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3as4 RCSB], [https://www.ebi.ac.uk/pdbsum/3as4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3as4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MAMA_MAGSA MAMA_MAGSA] Probably forms a large homooligomer on which other magnetosome subunits assemble (Probable). Required for formation of functional magnetosomes from pre-existing vesicles, it has a dynamic location in the cell (PubMed:15004275).<ref>PMID:15004275</ref> <ref>PMID:21784982</ref> 
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== Publication Abstract from PubMed ==
The magnetosome, a biomineralizing organelle within magnetotactic bacteria, allows their navigation along geomagnetic fields. Magnetosomes are membrane-bound compartments containing magnetic nanoparticles and organized into a chain within the cell, the assembly and biomineralization of magnetosomes are controlled by magnetosome-associated proteins. Here, we describe the crystal structures of the magnetosome-associated protein, MamA, from Magnetospirillum magneticum AMB-1 and Magnetospirillum gryphiswaldense MSR-1. MamA folds as a sequential tetra-trico-peptide repeat (TPR) protein with a unique hook-like shape. Analysis of the MamA structures indicates two distinct domains that can undergo conformational changes. Furthermore, structural analysis of seven crystal forms verified that the core of MamA is not affected by crystallization conditions and identified three protein-protein interaction sites, namely a concave site, a convex site, and a putative TPR repeat. Additionally, relying on transmission electron microscopy and size exclusion chromatography, we show that highly stable complexes form upon MamA homooligomerization. Disruption of the MamA putative TPR motif or N-terminal domain led to protein mislocalization in vivo and prevented MamA oligomerization in vitro. We, therefore, propose that MamA self-assembles through its putative TPR motif and its concave site to create a large homooligomeric scaffold which can interact with other magnetosome-associated proteins via the MamA convex site. We discuss the structural basis for TPR homooligomerization that allows the proper function of a prokaryotic organelle.

Self-recognition mechanism of MamA, a magnetosome-associated TPR-containing protein, promotes complex assembly.,Zeytuni N, Ozyamak E, Ben-Harush K, Davidov G, Levin M, Gat Y, Moyal T, Brik A, Komeili A, Zarivach R Proc Natl Acad Sci U S A. 2011 Aug 16;108(33):E480-7. Epub 2011 Jul 22. PMID:21784982<ref>PMID:21784982</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3as4" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Magnetospirillum magneticum AMB-1]]
[[Category: Davidov G]]
[[Category: Zarivach R]]
[[Category: Zeytuni N]]