Solution structure of a late embryogenesis abundant protein (LEA14) from Arabidopsis thaliana, a cellular stress-related protein

被引:89
作者
Singh, S
Cornilescu, CC
Tyler, RC
Cornilescu, G
Tonelli, M
Lee, MS
Markley, JL
机构
[1] Univ Wisconsin, Ctr Eukaryot Struct Genom, Dept Biochem, Madison, WI 53706 USA
[2] Univ Wisconsin, Natl Magnet Resonance Facil Madison, Dept Biochem, Madison, WI 53706 USA
关键词
LEA; LEA14; NMR spectroscopy; structural genomics; fibronectin Type III fold;
D O I
10.1110/ps.051579205
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
We report the three-dimensional structure of a late embryogenesis abundant (LEA) protein from Arabidopsis thaliana gene At1g01470.1. This protein is a member of Pfam cluster PF03168, and has been classified as a LEA14 protein. LEA proteins are expressed under conditions of cellular stress, such as desiccation, cold, osmotic stress, and heat. The structure, which was determined by NMR spectroscopy, revealed that the At1g01470.1 protein has an alpha beta-fold consisting of one alpha-helix and seven beta-strands that form two antiparallel beta-sheets. The closest structural homologs were discovered to be fibronectin Type III domains, which have < 7% sequence identity. Because fibronectins from animal cells have been shown to be involved in cell adhesion, cell motility, wound heating, and maintenance of cell shape, it is interesting to note that in plants wounding or stress results in the overexpression of a protein with fibronectin Type III structural features.
引用
收藏
页码:2601 / 2609
页数:9
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