1xfl
From Proteopedia
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'''Solution Structure of Thioredoxin h1 from Arabidopsis Thaliana''' | '''Solution Structure of Thioredoxin h1 from Arabidopsis Thaliana''' | ||
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[[Category: Vinarov, D.]] | [[Category: Vinarov, D.]] | ||
[[Category: Volkman, B F.]] | [[Category: Volkman, B F.]] | ||
| - | [[Category: | + | [[Category: At3g51030]] |
| - | [[Category: | + | [[Category: Center for eukaryotic structural genomic]] |
| - | [[Category: | + | [[Category: Cesg]] |
| - | [[Category: | + | [[Category: Electron transport]] |
| - | [[Category: | + | [[Category: Protein structure initiative]] |
| - | [[Category: | + | [[Category: Psi]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
| - | [[Category: | + | [[Category: Thioredoxin]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 30 13:22:29 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 10:22, 30 April 2008
Solution Structure of Thioredoxin h1 from Arabidopsis Thaliana
Overview
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.
About this Structure
1XFL is a Single protein structure of sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.
Reference
Solution structure of thioredoxin h1 from Arabidopsis thaliana., Peterson FC, Lytle BL, Sampath S, Vinarov D, Tyler E, Shahan M, Markley JL, Volkman BF, Protein Sci. 2005 Aug;14(8):2195-200. Epub 2005 Jun 29. PMID:15987893 Page seeded by OCA on Wed Apr 30 13:22:29 2008
Categories: Arabidopsis thaliana | Single protein | CESG, Center for Eukaryotic Structural Genomics. | Lytle, B L. | Markley, J L. | Peterson, F C. | Sampath, S. | Shahan, M. | Tyler, E. | Vinarov, D. | Volkman, B F. | At3g51030 | Center for eukaryotic structural genomic | Cesg | Electron transport | Protein structure initiative | Psi | Structural genomic | Thioredoxin
