4CMY

Chlorobium tepidum Ferritin

4CMY の概要

• エントリーDOI: 10.2210/pdb4cmy/pdb
• 分子名称: FERRITIN, FE (III) ION, ... (4 entities in total)
• 機能のキーワード: metal transport, iron-storage protein, iron metabolism
• 由来する生物種: CHLOROBACULUM TEPIDUM; 詳細
• 細胞内の位置: Cytoplasm : Q8KBP5 Q8KBP5
• タンパク質・核酸の鎖数: 24
• 化学式量合計: 566546.21

構造登録者

Pohl, E.,Arenas, M.,Townsend, P.D.,Yevenes, A. (登録日: 2014-01-18, 公開日: 2014-11-26, 最終更新日: 2024-05-08)

主引用文献

Arenas, M.,Townsend, P.D.,Brito, C.,Marquez, V.,Marabolli, V.,Gonzalez-Nilo, F.,Matias, C.,Watt, R.K.,Lopez-Castro, J.D.,Dominguez-Vera, J.,Pohl, E.,Yevenes, A.
The Crystal Structure of Ferritin from Chlorobium Tepidum Reveals a New Conformation of the 4-Fold Channel for This Protein Family.
Biochimie, 106:39-, 2014

PubMed 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 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.

PubMed: 25079050
DOI: 10.1016/J.BIOCHI.2014.07.019

実験手法

X-RAY DIFFRACTION (2.59 Å)