3vty: Difference between revisions
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==Crystal structure of MamA== | ==Crystal structure of MamA== | ||
<StructureSection load='3vty' size='340' side='right' caption='[[3vty]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='3vty' size='340' side='right'caption='[[3vty]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3vty]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3vty]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"candidatus_magnetobacterium_bavaricum"_spring_et_al_1993_in_spring_and_schleifer_2001 "candidatus magnetobacterium bavaricum" spring et al 1993 in spring and schleifer 2001]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VTY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VTY FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3vtx|3vtx]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3vtx|3vtx]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MamA ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MamA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29290 "Candidatus Magnetobacterium bavaricum" Spring et al 1993 in Spring and Schleifer 2001])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3vty FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vty OCA], [https://pdbe.org/3vty PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vty RCSB], [https://www.ebi.ac.uk/pdbsum/3vty PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vty ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Candidatus magnetobacterium bavaricum spring et al 1993 in spring and schleifer 2001]] | [[Category: Candidatus magnetobacterium bavaricum spring et al 1993 in spring and schleifer 2001]] | ||
[[Category: Large Structures]] | |||
[[Category: Baran, D]] | [[Category: Baran, D]] | ||
[[Category: Davidov, G]] | [[Category: Davidov, G]] | ||
Revision as of 22:04, 27 July 2022
Crystal structure of MamACrystal structure of MamA
Structural highlights
Publication Abstract from PubMedMagnetotactic 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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