Structural highlights
Function
FER_CHLRE Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Publication Abstract from PubMed
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.
NMR structures of ferredoxin chloroplastic transit peptide from Chlamydomonas reinhardtii promoted by trifluoroethanol in aqueous solution.,Lancelin JM, Bally I, Arlaud GJ, Blackledge M, Gans P, Stein M, Jacquot JP FEBS Lett. 1994 May 2;343(3):261-6. PMID:8174712[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lancelin JM, Bally I, Arlaud GJ, Blackledge M, Gans P, Stein M, Jacquot JP. NMR structures of ferredoxin chloroplastic transit peptide from Chlamydomonas reinhardtii promoted by trifluoroethanol in aqueous solution. FEBS Lett. 1994 May 2;343(3):261-6. PMID:8174712
