Structural characterization of bacterioferritin from Blastochloris viridis.

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....

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Autores principales:	Weixiao Y Wahlgren, Hadil Omran, David von Stetten, Antoine Royant, Sjoerd van der Post, Gergely Katona
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/51465b78002e45818e1559897f351ed7
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spelling	oai:doaj.org-article:51465b78002e45818e1559897f351ed72021-11-18T08:12:41ZStructural characterization of bacterioferritin from Blastochloris viridis.1932-620310.1371/journal.pone.0046992https://doaj.org/article/51465b78002e45818e1559897f351ed72012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23056552/?tool=EBIhttps://doaj.org/toc/1932-6203Iron 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.Weixiao Y WahlgrenHadil OmranDavid von StettenAntoine RoyantSjoerd van der PostGergely KatonaPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 10, p e46992 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Weixiao Y Wahlgren Hadil Omran David von Stetten Antoine Royant Sjoerd van der Post Gergely Katona Structural characterization of bacterioferritin from Blastochloris viridis.
description	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.
format	article
author	Weixiao Y Wahlgren Hadil Omran David von Stetten Antoine Royant Sjoerd van der Post Gergely Katona
author_facet	Weixiao Y Wahlgren Hadil Omran David von Stetten Antoine Royant Sjoerd van der Post Gergely Katona
author_sort	Weixiao Y Wahlgren
title	Structural characterization of bacterioferritin from Blastochloris viridis.
title_short	Structural characterization of bacterioferritin from Blastochloris viridis.
title_full	Structural characterization of bacterioferritin from Blastochloris viridis.
title_fullStr	Structural characterization of bacterioferritin from Blastochloris viridis.
title_full_unstemmed	Structural characterization of bacterioferritin from Blastochloris viridis.
title_sort	structural characterization of bacterioferritin from blastochloris viridis.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/51465b78002e45818e1559897f351ed7
work_keys_str_mv	AT weixiaoywahlgren structuralcharacterizationofbacterioferritinfromblastochlorisviridis AT hadilomran structuralcharacterizationofbacterioferritinfromblastochlorisviridis AT davidvonstetten structuralcharacterizationofbacterioferritinfromblastochlorisviridis AT antoineroyant structuralcharacterizationofbacterioferritinfromblastochlorisviridis AT sjoerdvanderpost structuralcharacterizationofbacterioferritinfromblastochlorisviridis AT gergelykatona structuralcharacterizationofbacterioferritinfromblastochlorisviridis
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Structural characterization of bacterioferritin from Blastochloris viridis.

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