2LIR

NMR Solution Structure of Yeast Iso-1-cytochrome c Mutant P71H in oxidized states

2LIR の概要

• エントリーDOI: 10.2210/pdb2lir/pdb
• 関連するPDBエントリー: 2LIT
• NMR情報: BMRB: 17903
• 分子名称: Cytochrome c iso-1, HEME C (2 entities in total)
• 機能のキーワード: cytochrome c, p71h, oxidized, metal transport
• 由来する生物種: Saccharomyces cerevisiae S288c (Baker's yeast)
• 細胞内の位置: Mitochondrion intermembrane space: P00044
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12673.23

構造登録者

Lan, W.,Wang, Z.,Yang, Z.,Zhu, J.,Ying, T.,Jiang, X.,Zhang, X.,Wu, H.,Liu, M.,Tan, X.,Cao, C.,Huang, Z.X. (登録日: 2011-08-31, 公開日: 2011-12-07, 最終更新日: 2024-11-06)

主引用文献

Lan, W.,Wang, Z.,Yang, Z.,Zhu, J.,Ying, T.,Jiang, X.,Zhang, X.,Wu, H.,Liu, M.,Tan, X.,Cao, C.,Huang, Z.X.
Conformational toggling of yeast iso-1-cytochrome C in the oxidized and reduced States.
Plos One, 6:e27219-e27219, 2011

PubMed Abstract: To convert cyt c into a peroxidase-like metalloenzyme, the P71H mutant was designed to introduce a distal histidine. Unexpectedly, its peroxidase activity was found even lower than that of the native, and that the axial ligation of heme iron was changed to His71/His18 in the oxidized state, while to Met80/His18 in the reduced state, characterized by UV-visible, circular dichroism, and resonance Raman spectroscopy. To further probe the functional importance of Pro71 in oxidation state dependent conformational changes occurred in cyt c, the solution structures of P71H mutant in both oxidation states were determined. The structures indicate that the half molecule of cyt c (aa 50-102) presents a kind of "zigzag riveting ruler" structure, residues at certain positions of this region such as Pro71, Lys73 can move a big distance by altering the tertiary structure while maintaining the secondary structures. This finding provides a molecular insight into conformational toggling in different oxidation states of cyt c that is principle significance to its biological functions in electron transfer and apoptosis. Structural analysis also reveals that Pro71 functions as a key hydrophobic patch in the folding of the polypeptide of the region (aa 50-102), to prevent heme pocket from the solvent.

PubMed: 22087268
DOI: 10.1371/journal.pone.0027219

実験手法

SOLUTION NMR