1Z6O

Crystal Structure of Trichoplusia ni secreted ferritin

1Z6O の概要

• エントリーDOI: 10.2210/pdb1z6o/pdb
• 分子名称: Ferritin light chain, Ferritin heavy chain, FE (III) ION, ... (5 entities in total)
• 機能のキーワード: metal binding protein, iron storage
• 由来する生物種: Trichoplusia ni (cabbage looper); 詳細
• タンパク質・核酸の鎖数: 24
• 化学式量合計: 554916.43

構造登録者

Hamburger, A.E.,West Jr., A.P.,Hamburger, Z.A.,Hamburger, P.,Bjorkman, P.J. (登録日: 2005-03-22, 公開日: 2005-05-24, 最終更新日: 2024-11-20)

主引用文献

Hamburger, A.E.,West, A.P.,Hamburger, Z.A.,Hamburger, P.,Bjorkman, P.J.
Crystal structure of a secreted insect ferritin reveals a symmetrical arrangement of heavy and light chains.
J.Mol.Biol., 349:558-569, 2005

PubMed Abstract: Ferritins are iron storage proteins made of 24 subunits forming a hollow spherical shell. Vertebrate ferritins contain varying ratios of heavy (H) and light (L) chains; however, known ferritin structures include only one type of chain and have octahedral symmetry. Here, we report the 1.9A structure of a secreted insect ferritin from Trichoplusia ni, which reveals equal numbers of H and L chains arranged with tetrahedral symmetry. The H/L-chain interface includes complementary features responsible for ordered assembly of the subunits. The H chain contains a ferroxidase active site resembling that of vertebrate H chains with an endogenous, bound iron atom. The L chain lacks the residues that form a putative iron core nucleation site in vertebrate L chains. Instead, a possible nucleation site is observed at the L chain 3-fold pore. The structure also reveals inter- and intrasubunit disulfide bonds, mostly in the extended N-terminal regions unique to insect ferritins. The symmetrical arrangement of H and L chains and the disulfide crosslinks reflect adaptations of insect ferritin to its role as a secreted protein.

PubMed: 15896348
DOI: 10.1016/j.jmb.2005.03.074

実験手法

X-RAY DIFFRACTION (1.91 Å)