3VNX

Crystal structure of ferritin from multicellular green algae, Ulva pertusa.

3VNX の概要

• エントリーDOI: 10.2210/pdb3vnx/pdb
• 分子名称: ferritin, CALCIUM ION (3 entities in total)
• 機能のキーワード: 4-helix bundle, iron storage, oxidoreductase
• 由来する生物種: Ulva pertusa
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23037.92

構造登録者

Masuda, T.,Morimoto, S.I.,Mikami, B.,Toyohara, H. (登録日: 2012-01-18, 公開日: 2012-03-28, 最終更新日: 2024-03-20)

主引用文献

Masuda, T.,Morimoto, S.I.,Mikami, B.,Toyohara, H.
The extension peptide of plant ferritin from sea lettuce contributes to shell stability and surface hydrophobicity.
Protein Sci., 21:786-796, 2012

PubMed Abstract: Plant ferritins have some unique structural and functional features. Most of these features can be related to the plant-specific "extension peptide" (EP), which exists in the N-terminus of the mature region of a plant ferritin. Recent crystallographic analysis of a plant ferritin revealed the structure of the EP, however, two points remain unclear: (i) whether the structures of well-conserved EP of plant ferritins are common in all plants, and (ii) whether the EP truly contributes to the shell stability of the plant ferritin oligomer. To clarify these matters, we have cloned a green-plant-type ferritin cDNA from a green alga, Ulva pertusa, and investigated its crystal structure. Ulva pertusa ferritin (UpFER) has a plant-ferritin-specific extension peptide composed of 28 amino acid residues. In the crystal structure of UpFER, the EP lay on and interacted with the neighboring threefold symmetry-related subunit. The amino acid residues involved in the interaction were very highly conserved among plant ferritins. The EPs masked the hydrophobic pockets on the ferritin shell surface by lying on them, and this made the ferritin oligomer more hydrophilic. Furthermore, differential scanning calorimetric analysis of the native and its EP-deletion mutant suggested that the EP contributed to the thermal stability of the plant ferritin shell. Thus, the shell stability and surface hydrophobicity of plant ferritin were controlled by the presence or absence of the plant-ferritin-specific EP. This regulation can account for those processes such as shell stability, degradation, and association of plant ferritin, which are significantly related to iron utilization in plants.

PubMed: 22419613
DOI: 10.1002/pro.2061

実験手法

X-RAY DIFFRACTION (2.4 Å)