1FCT

NMR STRUCTURES OF FERREDOXIN CHLOROPLASTIC TRANSIT PEPTIDE FROM CHLAMYDOMONAS REINHARDTII PROMOTED BY TRIFLUOROETHANOL IN AQUEOUS SOLUTION

1FCT の概要

• エントリーDOI: 10.2210/pdb1fct/pdb
• 分子名称: FERREDOXIN CHLOROPLASTIC TRANSIT PEPTIDE SEQUENCE FROM THE GREEN ALGA (1 entity in total)
• 機能のキーワード: transit peptide
• 由来する生物種: Chlamydomonas reinhardtii
• 細胞内の位置: Plastid, chloroplast: P07839
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3348.09

構造登録者

Lancelin, J.-M.,Blackledge, M. (登録日: 1994-03-30, 公開日: 1994-06-22, 最終更新日: 2024-05-22)

主引用文献

Lancelin, J.M.,Bally, I.,Arlaud, G.J.,Blackledge, M.,Gans, P.,Stein, M.,Jacquot, J.P.
NMR structures of ferredoxin chloroplastic transit peptide from Chlamydomonas reinhardtii promoted by trifluoroethanol in aqueous solution.
FEBS Lett., 343:261-266, 1994

PubMed Abstract: The 32-amino acid transit peptide of the unicellular green alga Chlamydomonas reinhardtii ferredoxin has been synthesized and analysed by NMR spectroscopy and circular dichroism. The results show that while the peptide is unstructured in water, it undergoes an alpha-helix formation from residue 3 to 13 in a 30:70 molar-ratio mixture of 2,2,2-trifluoroethanol. The remainder of the peptide is still unstructured in CF3CD2OD/H2O mixtures, but is distributed on a side opposite to a hydrophobic ridge formed by Met5, Phe9 and Val13 on the induced alpha-helix. The NMR structures driven by 2,2,2-trifluoroethanol in aqueous solution, are discussed in terms of potent interactions with the chloroplast envelope and its translocation molecular machinery.

PubMed: 8174712
DOI: 10.1016/0014-5793(94)80568-7

実験手法

SOLUTION NMR