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

¹ Center for Eukaryotic Structural Genomics, and ² National Magnetic Resonance Facility at Madison, Department of Biochemistry, University of Wisconsin—Madison, Madison, Wisconsin 53706, USA

(RECEIVED May 8, 2005; FINAL REVISION July 7, 2005; ACCEPTED July 10, 2005)

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 -fold consisting of one -helix and seven -strands that form two antiparallel -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 healing, 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.

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

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.051579205.

Reprint requests to: John L. Markley, Department of Biochemistry, University of Wisconsin—Madison, 433 Babcock Drive, Madison, WI 53706, USA; e-mail: markley{at}nmrfam.wisc.edu; fax: (608) 262-3759.

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