4.6 Article

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

期刊

PROTEIN SCIENCE
卷 14, 期 10, 页码 2601-2609

出版社

WILEY
DOI: 10.1110/ps.051579205

关键词

LEA; LEA14; NMR spectroscopy; structural genomics; fibronectin Type III fold

资金

  1. NCRR NIH HHS [P41 RR02301, P41 RR002301] Funding Source: Medline
  2. NIGMS NIH HHS [P50 GM64598, P41 GM66326, P41 GM066326, P50 GM064598] Funding Source: Medline

向作者/读者索取更多资源

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.

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