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Solution structure of the Thioredoxin h1 from poplar, a CPPC active site variantSolution structure of the Thioredoxin h1 from poplar, a CPPC active site variant
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedAssignment of heteronuclear and homonuclear multidimensional NMR spectra permits determination of the first three-dimensional solution structure of a higher-plant thioredoxin h. The collection of 1906 distance restraints, 137 TALOS-derived dihedral restraints, and 66 hydrogen bonds was used in the restrained molecular dynamics protocol to calculate the structure of the reduced form of thioredoxin h1 from poplar with an atomic rmsd of 0.60 +/- 0.12 A. This enzyme exhibits an unusual active site with the sequence WCPPC and original properties in terms of stability and specificity. Compared to other known thioredoxin structures, thioredoxin h1 from poplar adopts the classical "Trx fold". Its atypical active site possesses a conformation similar to that of other common thioredoxins but appears to be more rigid. Moreover, the hydrogen bond network, stabilizing the in-core beta-sheet, is tighter than in Chlamydomonas reinhardtii, explaining the difference in thermostability. Solution structure of a natural CPPC active site variant, the reduced form of thioredoxin h1 from poplar.,Coudevylle N, Thureau A, Hemmerlin C, Gelhaye E, Jacquot JP, Cung MT Biochemistry. 2005 Feb 15;44(6):2001-8. PMID:15697225[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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