1XFL

Solution Structure of Thioredoxin h1 from Arabidopsis Thaliana

Summary for 1XFL

• Entry DOI: 10.2210/pdb1xfl/pdb
• NMR Information: BMRB: 6318
• Descriptor: Thioredoxin h1 (1 entity in total)
• Functional Keywords: at3g51030, thioredoxin, structural genomics, protein structure initiative, cesg, psi, center for eukaryotic structural genomics, electron transport
• Biological source: Arabidopsis thaliana (thale cress)
• Cellular location: Cytoplasm (By similarity): P29448
• Total number of polymer chains: 1
• Total formula weight: 13947.10

Authors

Peterson, F.C.,Lytle, B.L.,Sampath, S.,Vinarov, D.,Tyler, E.,Shahan, M.,Markley, J.L.,Volkman, B.F.,Center for Eukaryotic Structural Genomics (CESG) (deposition date: 2004-09-15, release date: 2004-09-28, Last modification date: 2024-10-30)

Primary citation

Peterson, F.C.,Lytle, B.L.,Sampath, S.,Vinarov, D.,Tyler, E.,Shahan, M.,Markley, J.L.,Volkman, B.F.
Solution structure of thioredoxin h1 from Arabidopsis thaliana.
Protein Sci., 14:2195-2200, 2005

PubMed Abstract: Present in virtually every species, thioredoxins catalyze disulfide/dithiol exchange with various substrate proteins. While the human genome contains a single thioredoxin gene, plant thioredoxins are a complex protein family. A total of 19 different thioredoxin genes in six subfamilies has emerged from analysis of the Arabidopsis thaliana genome. Some function specifically in mitochondrial and chloroplast redox signaling processes, but target substrates for a group of eight thioredoxin proteins comprising the h subfamily are largely uncharacterized. In the course of a structural genomics effort directed at the recently completed A. thaliana genome, we determined the structure of thioredoxin h1 (At3g51030.1) in the oxidized state. The structure, defined by 1637 NMR-derived distance and torsion angle constraints, displays the conserved thioredoxin fold, consisting of a five-stranded beta-sheet flanked by four helices. Redox-dependent chemical shift perturbations mapped primarily to the conserved WCGPC active-site sequence and other nearby residues, but distant regions of the C-terminal helix were also affected by reduction of the active-site disulfide. Comparisons of the oxidized A. thaliana thioredoxin h1 structure with an h-type thioredoxin from poplar in the reduced state revealed structural differences in the C-terminal helix but no major changes in the active site conformation.

PubMed: 15987893
DOI: 10.1110/ps.051477905

Experimental method

SOLUTION NMR