title: Solution structure of At3g04780.1-des15, an Arabidopsis thaliana ortholog of the C-terminal domain of human thioredoxin-like protein.
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.
authors.affiliation: Center for Eukaryotic Structural Genomics, Department of Biochemistry, 433 Babcock Drive, University of Wisconsin-Madison, Madison, WI 53706-1544, USA.
authors.forename: Jikui
authors.initials: J
authors.lastname: Song
authors.forename: Robert C
authors.initials: RC
authors.lastname: Tyler
authors.forename: Russell L
authors.initials: RL
authors.lastname: Wrobel
authors.forename: Ronnie O
authors.initials: RO
authors.lastname: Frederick
authors.forename: Frank C
authors.initials: FC
authors.lastname: Vojtek
authors.forename: Won Bae
authors.initials: WB
authors.lastname: Jeon
authors.forename: Min S
authors.initials: MS
authors.lastname: Lee
authors.forename: John L
authors.initials: JL
authors.lastname: Markley
mesh_terms: D029681:Arabidopsis Proteins / Q000737:chemistry*; D006801:Humans; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D017434:Protein Structure, Tertiary; D013879:Thioredoxins / Q000737:chemistry*
chemical_list: D029681:Arabidopsis Proteins; C502370:At3g04780.1-des15 protein, Arabidopsis; D013879:Thioredoxins
references.citation: J Mol Biol. 2002 May 24;319(1):209-27
references.pmid: 12051947
references.citation: Protein Expr Purif. 2005 Apr;40(2):268-78
references.pmid: 15766868
references.citation: J Biomol NMR. 1999 Mar;13(3):289-302
references.pmid: 10212987
references.citation: J Magn Reson. 2003 Jan;160(1):65-73
references.pmid: 12565051
references.citation: Nat Struct Biol. 2000 Nov;7 Suppl:935-9
references.pmid: 11103992
references.citation: J Biol Chem. 1998 Jul 24;273(30):19160-6
references.pmid: 9668102
references.citation: J Mol Biol. 1997 Oct 17;273(1):283-98
references.pmid: 9367762
references.citation: Eur J Biochem. 2002 Apr;269(8):2060-8
references.pmid: 11985582
references.citation: DNA Seq. 2000;10(6):419-24
references.pmid: 10826702
references.citation: J Mol Graph. 1996 Feb;14(1):51-5, 29-32
references.pmid: 8744573
references.citation: J Struct Funct Genomics. 2005;6(2-3):143-7
references.pmid: 16211511
references.citation: Curr Opin Chem Biol. 2001 Aug;5(4):402-8
references.pmid: 11470603
references.citation: Structure. 1996 Jun 15;4(6):735-51
references.pmid: 8805557
references.citation: J Biomol NMR. 1996 May;7(3):207-13
references.pmid: 22911044
references.citation: J Biomol NMR. 1996 Dec;8(4):477-86
references.pmid: 9008363
references.citation: Nat Struct Biol. 2002 Aug;9(8):628-34
references.pmid: 12091873
references.citation: Nature. 1991 Mar 7;350(6313):87-90
references.pmid: 2002850
references.citation: J Biomol NMR. 2004 Oct;30(2):215-8
references.pmid: 15702529
references.citation: J Mol Biol. 2002 Mar 1;316(4):955-68
references.pmid: 11884135