Premium
Three‐dimensional structure and mimetic‐membrane association of consensus 11‐amino‐acid motif from soybean lea3 protein
Author(s) -
Xue Rong,
Liu Yun,
Zheng Yizhi,
Wu Yijie,
Li Xiaojing,
Pei Fengkui,
Ni Jiazuan
Publication year - 2011
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.21693
Subject(s) - chemistry , micelle , structural motif , membrane , crystallography , sequence motif , protein secondary structure , motif (music) , stereochemistry , biophysics , biochemistry , aqueous solution , organic chemistry , gene , physics , biology , acoustics
The occurrence of a highly conserved 11‐mer repeating motif in the primary sequence is a major characteristic of group 3 late embryogenesis abundant (LEA3) proteins, which are strongly associated with abiotic stress tolerance of the plants. In this study, the three‐dimensional structure, mimetic membrane association, and salt effect for consensus 11‐mer motif from soybean PM2 protein (LEA3) were investigated in sodium dodecyl sulfate (SDS) micelles by NMR techniques. It was shown that the 11‐mer motif was disordered in aqueous solution, but adopted an α‐helix in SDS micelles. NMR diffusion measurements demonstrated that the 11‐mer motif was associated with SDS micelles. Paramagnetic quenching NMR experiments further revealed the orientation of the 11‐mer motif with respect to the mimetic membrane: the ordered N‐terminal segment was inserted into the mimetic membrane, and the disordered C‐terminal segment was exposed to water. In addition, salt addition could not change the secondary structure of the 11‐mer motif, but might slightly alter the relative spatial position of some N‐terminal residue atoms. These results implied that the 11‐mer motif would take an important role in structural plasticity and membrane stabilization for LEA3 proteins. © 2011 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 98: 59–66, 2012.