View source for 4am4


==Bacterioferritin from Blastochloris viridis==
<StructureSection load='4am4' size='340' side='right'caption='[[4am4]], [[Resolution|resolution]] 1.68&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4am4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Blastochloris_viridis Blastochloris viridis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AM4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AM4 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4am2|4am2]]</div></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=4am4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4am4 OCA], [https://pdbe.org/4am4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4am4 RCSB], [https://www.ebi.ac.uk/pdbsum/4am4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4am4 ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Iron storage and elimination of toxic ferrous iron are the responsibility of bacterioferritins in bacterial species. Bacterioferritins are capable of oxidizing iron using molecular oxygen and import iron ions into the large central cavity of the protein, where they are stored in a mineralized form. We isolated, crystallized bacterioferritin from the microaerophilic/anaerobic, purple non-sulfur bacterium Blastochloris viridis and determined its amino acid sequence and X-ray structure. The structure and sequence revealed similarity to other purple bacterial species with substantial differences in the pore regions. Static 3- and 4-fold pores do not allow the passage of iron ions even though structural dynamics may assist the iron gating. On the other hand the B-pore is open to water and larger ions in its native state. In order to study the mechanism of iron import, multiple soaking experiments were performed. Upon Fe(II) and urea treatment the ferroxidase site undergoes reorganization as seen in bacterioferritin from Escherichia coli and Pseudomonas aeruginosa. When soaking with Fe(II) only, a closely bound small molecular ligand is observed close to Fe(1) and the coordination of Glu94 to Fe(2) changes from bidentate to monodentate. DFT calculations indicate that the bound ligand is most likely a water or a hydroxide molecule representing a product complex. On the other hand the different soaking treatments did not modify the conformation of other pore regions.

Structural Characterization of Bacterioferritin from Blastochloris viridis.,Wahlgren WY, Omran H, von Stetten D, Royant A, van der Post S, Katona G PLoS One. 2012;7(10):e46992. doi: 10.1371/journal.pone.0046992. Epub 2012 Oct 9. PMID:23056552<ref>PMID:23056552</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 4am4" style="background-color:#fffaf0;"></div>

==See Also==
*[[Ferritin 3D structures|Ferritin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Blastochloris viridis]]
[[Category: Large Structures]]
[[Category: Katona, G]]
[[Category: Omran, H]]
[[Category: Post, S van der]]
[[Category: Royant, A]]
[[Category: Stetten, D von]]
[[Category: Wahlgren, W Y]]
[[Category: Di iron centre]]
[[Category: Double-soaked]]
[[Category: Ferroxidase centre]]
[[Category: Heme binding]]
[[Category: Iron channel]]
[[Category: Iron storage]]
[[Category: Metal binding protein]]