1ti3
From Proteopedia
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| - | [[Image:1ti3.gif|left|200px]] | + | [[Image:1ti3.gif|left|200px]] |
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| - | '''Solution structure of the Thioredoxin h1 from poplar, a CPPC active site variant''' | + | {{Structure |
| + | |PDB= 1ti3 |SIZE=350|CAPTION= <scene name='initialview01'>1ti3</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Solution structure of the Thioredoxin h1 from poplar, a CPPC active site variant''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1TI3 is a [ | + | 1TI3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Populus_tremula Populus tremula]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TI3 OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15697225 15697225] |
[[Category: Populus tremula]] | [[Category: Populus tremula]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: thioredoxin]] | [[Category: thioredoxin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:18:37 2008'' |
Revision as of 12:18, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Solution structure of the Thioredoxin h1 from poplar, a CPPC active site variant
Overview
Assignment 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.
About this Structure
1TI3 is a Single protein structure of sequence from Populus tremula. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 14:18:37 2008
