1xfl
From Proteopedia
| Line 4: | Line 4: | ||
==Overview== | ==Overview== | ||
| - | Present in virtually every species, thioredoxins catalyze | + | 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== | ==About this Structure== | ||
| Line 13: | Line 13: | ||
[[Category: Arabidopsis thaliana]] | [[Category: Arabidopsis thaliana]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: CESG, Center | + | [[Category: CESG, Center for Eukaryotic Structural Genomics.]] |
| - | [[Category: Lytle, B | + | [[Category: Lytle, B L.]] |
| - | [[Category: Markley, J | + | [[Category: Markley, J L.]] |
| - | [[Category: Peterson, F | + | [[Category: Peterson, F C.]] |
[[Category: Sampath, S.]] | [[Category: Sampath, S.]] | ||
[[Category: Shahan, M.]] | [[Category: Shahan, M.]] | ||
[[Category: Tyler, E.]] | [[Category: Tyler, E.]] | ||
[[Category: Vinarov, D.]] | [[Category: Vinarov, D.]] | ||
| - | [[Category: Volkman, B | + | [[Category: Volkman, B F.]] |
[[Category: at3g51030]] | [[Category: at3g51030]] | ||
[[Category: center for eukaryotic structural genomics]] | [[Category: center for eukaryotic structural genomics]] | ||
| Line 31: | Line 31: | ||
[[Category: thioredoxin]] | [[Category: thioredoxin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:54:15 2008'' |
Revision as of 13:54, 21 February 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 Thu Feb 21 15:54:15 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 genomics | Cesg | Electron transport | Protein structure initiative | Psi | Structural genomics | Thioredoxin
