View source for 4am5


==Bacterioferritin from Blastochloris viridis==
<StructureSection load='4am5' size='340' side='right'caption='[[4am5]], [[Resolution|resolution]] 1.58&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4am5]] 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=4AM5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AM5 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]] 1.58&#8491;</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4am5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4am5 OCA], [https://pdbe.org/4am5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4am5 RCSB], [https://www.ebi.ac.uk/pdbsum/4am5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4am5 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/K7N5M0_BLAVI K7N5M0_BLAVI] Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex.[PIRNR:PIRNR002560]
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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 4am5" 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: Royant A]]
[[Category: Wahlgren WY]]
[[Category: Van der Post S]]
[[Category: Von Stetten D]]