Solution structure of At3g04780.1-des15, an Arabidopsis thaliana ortholog of the C-terminal domain of human thioredoxin-like protein.
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.
Song
Jikui
J
Center for Eukaryotic Structural Genomics, Department of Biochemistry, 433 Babcock Drive, University of Wisconsin-Madison, Madison, WI 53706-1544, USA.
Tyler
Robert C
RC
Wrobel
Russell L
RL
Frederick
Ronnie O
RO
Vojtek
Frank C
FC
Jeon
Won Bae
WB
Lee
Min S
MS
Markley
John L
JL
D029681:Arabidopsis Proteins / Q000737:chemistry*; D006801:Humans; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D017434:Protein Structure, Tertiary; D013879:Thioredoxins / Q000737:chemistry*
D029681:Arabidopsis Proteins; C502370:At3g04780.1-des15 protein, Arabidopsis; D013879:Thioredoxins
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