1XFL

Solution Structure of Thioredoxin h1 from Arabidopsis Thaliana

1XFL の概要

• エントリーDOI: 10.2210/pdb1xfl/pdb
• NMR情報: BMRB: 6318
• 分子名称: Thioredoxin h1 (1 entity in total)
• 機能のキーワード: at3g51030, thioredoxin, structural genomics, protein structure initiative, cesg, psi, center for eukaryotic structural genomics, electron transport
• 由来する生物種: Arabidopsis thaliana (thale cress)
• 細胞内の位置: Cytoplasm (By similarity): P29448
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13947.10

構造登録者

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) (登録日: 2004-09-15, 公開日: 2004-09-28, 最終更新日: 2024-10-30)

主引用文献

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

実験手法

SOLUTION NMR