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3vtx

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==Crystal structure of MamA protein==
==Crystal structure of MamA protein==
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<StructureSection load='3vtx' size='340' side='right' caption='[[3vtx]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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<StructureSection load='3vtx' size='340' side='right'caption='[[3vtx]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3vtx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Candidatus_magnetobacterium_bavaricum Candidatus magnetobacterium bavaricum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VTX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VTX FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3vtx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Candidatus_Magnetobacterium_bavaricum Candidatus Magnetobacterium bavaricum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VTX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VTX FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3vty|3vty]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MamA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29290 Candidatus Magnetobacterium bavaricum])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3vtx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vtx OCA], [https://pdbe.org/3vtx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vtx RCSB], [https://www.ebi.ac.uk/pdbsum/3vtx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vtx ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3vtx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vtx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vtx RCSB], [http://www.ebi.ac.uk/pdbsum/3vtx PDBsum]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/K7N5L8_9BACT K7N5L8_9BACT]
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Magnetotactic bacteria enclose the magnetosome, a unique prokaryotic sub-cellular organelle that allows the biomineralization of magnetic nano-crystals. Membrane-coated magnetosomes are arranged into a linear chain that permits magnetotactic bacteria to navigate geomagnetic fields. Magnetosome assembly and biomineralization are controlled by conserved magnetosome-associated proteins, including MamA, a tetra-trico-peptide repeat (TPR)-containing protein that was shown to coat the magnetosome membrane. In this study, two MamA structures from Candidatus Magnetobacterium bavaricum (Mbav) were determined via X-ray crystallography. These structures confirm that Mbav MamA folds as a sequential TPR protein and shares a high degree of structural similarity with homologous MamA proteins from Magnetospirillum species. Furthermore, the two TPR-containing domains of MamA are separated by an interphylum-conserved region containing a flexible hinge that is involved in ligand binding and recognition. Finally, substantial differences were found in the local stabilization of the MamA N-terminal domain as a result of the loss of an evolutionary conserved salt bridge.
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Inter-phylum structural conservation of the magnetosome-associated TPR-containing protein, MamA.,Zeytuni N, Baran D, Davidov G, Zarivach R J Struct Biol. 2012 Dec;180(3):479-87. doi: 10.1016/j.jsb.2012.08.001. Epub 2012 , Aug 15. PMID:22917855<ref>PMID:22917855</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Candidatus magnetobacterium bavaricum]]
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[[Category: Candidatus Magnetobacterium bavaricum]]
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[[Category: Baran, D]]
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[[Category: Large Structures]]
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[[Category: Davidov, G]]
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[[Category: Baran D]]
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[[Category: Zarivach, R]]
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[[Category: Davidov G]]
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[[Category: Zeytuni, N]]
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[[Category: Zarivach R]]
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[[Category: Peptide binding protein]]
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[[Category: Zeytuni N]]
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[[Category: Protein binding]]
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Current revision

Crystal structure of MamA protein

PDB ID 3vtx

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