Protein Sci. 2005 Apr;14(4):1059-63. Epub 2005 Mar 1.

Solution structure of At3g04780.1-des15, an Arabidopsis thaliana ortholog of the C-terminal domain of human thioredoxin-like protein.

Song J, Tyler RC, Wrobel RL, Frederick RO, Vojtek FC, Jeon WB, Lee MS, Markley JL.

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Center for Eukaryotic Structural Genomics, Department of Biochemistry, 433 Babcock Drive, University of Wisconsin-Madison, Madison, WI 53706-1544, USA.

Abstract

The structure of At3g04780.1-des15, an Arabidopsis thaliana ortholog of the C-terminal domain of human thioredoxin-like protein, was determined by NMR spectroscopy. The structure is dominated by a beta-barrel sandwich. A two-stranded anti-parallel beta-sheet, which seals off one end of the beta-barrel, is flanked by two flexible loops rich in acidic amino acids. Although this fold often provides a ligand binding site, the structure did not reveal an appreciable cavity inside the beta-barrel. The three-dimensional structure of At3g04780.1-des15 provides an entry point for understanding its functional role and those of its mammalian homologs.

PMID:: 15741346; [PubMed - indexed for MEDLINE]
PMCID:: PMC2253455

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Structures reported by this article

Solution Structure Of At3g04780.1, An Arabidopsis Ortholog Of The C-Terminal Domain Of Human Thioredoxin-Like Protein

PDB: 1XOY

Source: Arabidopsis thaliana

Method: Solution Nmr

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