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| | ==Bacterioferritin from Blastochloris viridis== | | ==Bacterioferritin from Blastochloris viridis== |
| - | <StructureSection load='4am5' size='340' side='right' caption='[[4am5]], [[Resolution|resolution]] 1.58Å' scene=''> | + | <StructureSection load='4am5' size='340' side='right'caption='[[4am5]], [[Resolution|resolution]] 1.58Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4am5]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AM5 FirstGlance]. <br> | + | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.58Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4am4|4am4]], [[4am2|4am2]]</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4am5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4am5 OCA], [http://pdbe.org/4am5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4am5 RCSB], [http://www.ebi.ac.uk/pdbsum/4am5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4am5 ProSAT]</span></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> | | </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] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4am5" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4am5" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Ferritin 3D structures|Ferritin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Blastochloris viridis]] | | [[Category: Blastochloris viridis]] |
| - | [[Category: Katona, G]] | + | [[Category: Large Structures]] |
| - | [[Category: Omran, H]] | + | [[Category: Katona G]] |
| - | [[Category: Post, S van der]] | + | [[Category: Omran H]] |
| - | [[Category: Royant, A]] | + | [[Category: Royant A]] |
| - | [[Category: Stetten, D von]]
| + | [[Category: Wahlgren WY]] |
| - | [[Category: Wahlgren, W Y]] | + | [[Category: Van der Post S]] |
| - | [[Category: Di iron centre]] | + | [[Category: Von Stetten D]] |
| - | [[Category: Ferroxidase centre]] | + | |
| - | [[Category: Heme binding]]
| + | |
| - | [[Category: Iron channel]]
| + | |
| - | [[Category: Iron storage]]
| + | |
| - | [[Category: Metal binding protein]]
| + | |
| Structural highlights
Function
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]
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Wahlgren WY, Omran H, von Stetten D, Royant A, van der Post S, Katona G. Structural Characterization of Bacterioferritin from Blastochloris viridis. PLoS One. 2012;7(10):e46992. doi: 10.1371/journal.pone.0046992. Epub 2012 Oct 9. PMID:23056552 doi:http://dx.doi.org/10.1371/journal.pone.0046992
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