The crystal structure of ferritin from Chlorobium tepidum reveals a new conformation of the 4-fold channel for this protein family

Mauricio Arenas-Salinas, Philip D. Townsend, Christian Brito, Valeria Marquez, Vanessa Marabolli, Fernando Gonzalez-Nilo, Cata Matias, Richard K. Watt, Juan D. López-Castro, José Domínguez-Vera, Ehmke Pohl, Alejandro Yévenes

Resultado de la investigación: Article

5 Citas (Scopus)

Resumen

Ferritins are ubiquitous iron-storage proteins found in all kingdoms of life. They share a common architecture made of 24 subunits of five α-helices. The recombinant Chlorobium tepidum ferritin (rCtFtn) is a structurally interesting protein since sequence alignments with other ferritins show that this protein has a significantly extended C-terminus, which possesses 12 histidine residues as well as several aspartate and glutamic acid residues that are potential metal ion binding residues. We show that the macromolecular assembly of rCtFtn exhibits a cage-like hollow shell consisting of 24 monomers that are related by 4-3-2 symmetry; similar to the assembly of other ferritins. In all ferritins of known structure the short fifth α-helix adopts an acute angle with respect to the four-helix bundle. However, the crystal structure of the rCtFtn presented here shows that this helix adopts a new conformation defining a new assembly of the 4-fold channel of rCtFtn. This conformation allows the arrangement of the C-terminal region into the inner cavity of the protein shell. Furthermore, two Fe(III) ions were found in each ferroxidase center of rCtFtn, with an average FeA-FeB distance of 3 Å; corresponding to a diferric μ-oxo/hydroxo species. This is the first ferritin crystal structure with an isolated di-iron center in an iron-storage ferritin. The crystal structure of rCtFtn and the biochemical results presented here, suggests that rCtFtn presents similar biochemical properties reported for other members of this protein family albeit with distinct structural plasticity.

Idioma originalEnglish
Páginas (desde-hasta)39-47
Número de páginas9
PublicaciónBiochimie
Volumen106
DOI
EstadoPublished - 1 ene 2014

Huella dactilar

Chlorobium
Ferritins
Conformations
Crystal structure
Proteins
Iron
Ions
Ceruloplasmin
Sequence Alignment

ASJC Scopus subject areas

  • Biochemistry

Citar esto

Arenas-Salinas, Mauricio ; Townsend, Philip D. ; Brito, Christian ; Marquez, Valeria ; Marabolli, Vanessa ; Gonzalez-Nilo, Fernando ; Matias, Cata ; Watt, Richard K. ; López-Castro, Juan D. ; Domínguez-Vera, José ; Pohl, Ehmke ; Yévenes, Alejandro. / The crystal structure of ferritin from Chlorobium tepidum reveals a new conformation of the 4-fold channel for this protein family. En: Biochimie. 2014 ; Vol. 106. pp. 39-47.
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title = "The crystal structure of ferritin from Chlorobium tepidum reveals a new conformation of the 4-fold channel for this protein family",
abstract = "Ferritins are ubiquitous iron-storage proteins found in all kingdoms of life. They share a common architecture made of 24 subunits of five α-helices. The recombinant Chlorobium tepidum ferritin (rCtFtn) is a structurally interesting protein since sequence alignments with other ferritins show that this protein has a significantly extended C-terminus, which possesses 12 histidine residues as well as several aspartate and glutamic acid residues that are potential metal ion binding residues. We show that the macromolecular assembly of rCtFtn exhibits a cage-like hollow shell consisting of 24 monomers that are related by 4-3-2 symmetry; similar to the assembly of other ferritins. In all ferritins of known structure the short fifth α-helix adopts an acute angle with respect to the four-helix bundle. However, the crystal structure of the rCtFtn presented here shows that this helix adopts a new conformation defining a new assembly of the 4-fold channel of rCtFtn. This conformation allows the arrangement of the C-terminal region into the inner cavity of the protein shell. Furthermore, two Fe(III) ions were found in each ferroxidase center of rCtFtn, with an average FeA-FeB distance of 3 {\AA}; corresponding to a diferric μ-oxo/hydroxo species. This is the first ferritin crystal structure with an isolated di-iron center in an iron-storage ferritin. The crystal structure of rCtFtn and the biochemical results presented here, suggests that rCtFtn presents similar biochemical properties reported for other members of this protein family albeit with distinct structural plasticity.",
keywords = "Bacterial ferritin, Crystal structure, Ferroxidase center, HAADF-STEM",
author = "Mauricio Arenas-Salinas and Townsend, {Philip D.} and Christian Brito and Valeria Marquez and Vanessa Marabolli and Fernando Gonzalez-Nilo and Cata Matias and Watt, {Richard K.} and L{\'o}pez-Castro, {Juan D.} and Jos{\'e} Dom{\'i}nguez-Vera and Ehmke Pohl and Alejandro Y{\'e}venes",
year = "2014",
month = "1",
day = "1",
doi = "10.1016/j.biochi.2014.07.019",
language = "English",
volume = "106",
pages = "39--47",
journal = "Biochimie",
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Arenas-Salinas, M, Townsend, PD, Brito, C, Marquez, V, Marabolli, V, Gonzalez-Nilo, F, Matias, C, Watt, RK, López-Castro, JD, Domínguez-Vera, J, Pohl, E & Yévenes, A 2014, 'The crystal structure of ferritin from Chlorobium tepidum reveals a new conformation of the 4-fold channel for this protein family', Biochimie, vol. 106, pp. 39-47. https://doi.org/10.1016/j.biochi.2014.07.019

The crystal structure of ferritin from Chlorobium tepidum reveals a new conformation of the 4-fold channel for this protein family. / Arenas-Salinas, Mauricio; Townsend, Philip D.; Brito, Christian; Marquez, Valeria; Marabolli, Vanessa; Gonzalez-Nilo, Fernando; Matias, Cata; Watt, Richard K.; López-Castro, Juan D.; Domínguez-Vera, José; Pohl, Ehmke; Yévenes, Alejandro.

En: Biochimie, Vol. 106, 01.01.2014, p. 39-47.

Resultado de la investigación: Article

TY - JOUR

T1 - The crystal structure of ferritin from Chlorobium tepidum reveals a new conformation of the 4-fold channel for this protein family

AU - Arenas-Salinas, Mauricio

AU - Townsend, Philip D.

AU - Brito, Christian

AU - Marquez, Valeria

AU - Marabolli, Vanessa

AU - Gonzalez-Nilo, Fernando

AU - Matias, Cata

AU - Watt, Richard K.

AU - López-Castro, Juan D.

AU - Domínguez-Vera, José

AU - Pohl, Ehmke

AU - Yévenes, Alejandro

PY - 2014/1/1

Y1 - 2014/1/1

N2 - Ferritins are ubiquitous iron-storage proteins found in all kingdoms of life. They share a common architecture made of 24 subunits of five α-helices. The recombinant Chlorobium tepidum ferritin (rCtFtn) is a structurally interesting protein since sequence alignments with other ferritins show that this protein has a significantly extended C-terminus, which possesses 12 histidine residues as well as several aspartate and glutamic acid residues that are potential metal ion binding residues. We show that the macromolecular assembly of rCtFtn exhibits a cage-like hollow shell consisting of 24 monomers that are related by 4-3-2 symmetry; similar to the assembly of other ferritins. In all ferritins of known structure the short fifth α-helix adopts an acute angle with respect to the four-helix bundle. However, the crystal structure of the rCtFtn presented here shows that this helix adopts a new conformation defining a new assembly of the 4-fold channel of rCtFtn. This conformation allows the arrangement of the C-terminal region into the inner cavity of the protein shell. Furthermore, two Fe(III) ions were found in each ferroxidase center of rCtFtn, with an average FeA-FeB distance of 3 Å; corresponding to a diferric μ-oxo/hydroxo species. This is the first ferritin crystal structure with an isolated di-iron center in an iron-storage ferritin. The crystal structure of rCtFtn and the biochemical results presented here, suggests that rCtFtn presents similar biochemical properties reported for other members of this protein family albeit with distinct structural plasticity.

AB - Ferritins are ubiquitous iron-storage proteins found in all kingdoms of life. They share a common architecture made of 24 subunits of five α-helices. The recombinant Chlorobium tepidum ferritin (rCtFtn) is a structurally interesting protein since sequence alignments with other ferritins show that this protein has a significantly extended C-terminus, which possesses 12 histidine residues as well as several aspartate and glutamic acid residues that are potential metal ion binding residues. We show that the macromolecular assembly of rCtFtn exhibits a cage-like hollow shell consisting of 24 monomers that are related by 4-3-2 symmetry; similar to the assembly of other ferritins. In all ferritins of known structure the short fifth α-helix adopts an acute angle with respect to the four-helix bundle. However, the crystal structure of the rCtFtn presented here shows that this helix adopts a new conformation defining a new assembly of the 4-fold channel of rCtFtn. This conformation allows the arrangement of the C-terminal region into the inner cavity of the protein shell. Furthermore, two Fe(III) ions were found in each ferroxidase center of rCtFtn, with an average FeA-FeB distance of 3 Å; corresponding to a diferric μ-oxo/hydroxo species. This is the first ferritin crystal structure with an isolated di-iron center in an iron-storage ferritin. The crystal structure of rCtFtn and the biochemical results presented here, suggests that rCtFtn presents similar biochemical properties reported for other members of this protein family albeit with distinct structural plasticity.

KW - Bacterial ferritin

KW - Crystal structure

KW - Ferroxidase center

KW - HAADF-STEM

UR - http://www.scopus.com/inward/record.url?scp=84908021381&partnerID=8YFLogxK

U2 - 10.1016/j.biochi.2014.07.019

DO - 10.1016/j.biochi.2014.07.019

M3 - Article

C2 - 25079050

AN - SCOPUS:84908021381

VL - 106

SP - 39

EP - 47

JO - Biochimie

JF - Biochimie

SN - 0300-9084

ER -