1FCT

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

Summary for 1FCT

• Entry DOI: 10.2210/pdb1fct/pdb
• Descriptor: FERREDOXIN CHLOROPLASTIC TRANSIT PEPTIDE SEQUENCE FROM THE GREEN ALGA (1 entity in total)
• Functional Keywords: transit peptide
• Biological source: Chlamydomonas reinhardtii
• Cellular location: Plastid, chloroplast: P07839
• Total number of polymer chains: 1
• Total formula weight: 3348.09

Authors

Lancelin, J.-M.,Blackledge, M. (deposition date: 1994-03-30, release date: 1994-06-22, Last modification date: 2024-05-22)

Primary citation

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

Experimental method

SOLUTION NMR