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1gl8

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{{STRUCTURE_1gl8| PDB=1gl8 | SCENE= }}
{{STRUCTURE_1gl8| PDB=1gl8 | SCENE= }}
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'''SOLUTION STRUCTURE OF THIOREDOXIN M FROM SPINACH, OXIDIZED FORM'''
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===SOLUTION STRUCTURE OF THIOREDOXIN M FROM SPINACH, OXIDIZED FORM===
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==Overview==
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Proton NMR spectral resonances of thioredoxin m from spinach have been assigned, and its solution structure has been determined on the basis of 1156 nuclear Overhauser effect- (NOE-) derived distance constraints by using restrained molecular dynamics calculations. The average pairwise root-mean-square deviation (RMSD) for the 25 best NMR structures for the backbone was 1.0 +/- 0.1, when the structurally well-defined residues were considered. The N- and C-terminal segments (1-13 and 118-119) and residues 41-49, comprising the active site, are highly disordered. At the time of concluding this work, a crystal structure of this protein was reported, in which thioredoxin m was found to crystallize as noncovalent dimers. Although the solution and crystal structures are very similar, no evidence was found about the existence of dimers in solution, thus confirming that dimerization is not needed for the regulatory activity of thioredoxin m. The spinach thioredoxin m does not unfold by heat in the range 25-85 degrees C, as revealed by thermal circular dichroic (CD) measurements. However, its unfolding free energy (9.1 +/- 0.8 kcal mol(-1), at pH 5.3 and 25 degrees C) could be determined by extrapolating the free energy values obtained at different concentrations of guanidinium chloride (GdmCl). The folding-unfolding process is two-state as indicated by the coincidence of the CD denaturation curves obtained at far and near UV. The H/D exchange behavior of backbone amide protons was analyzed. The slowest-exchanging protons, requiring a global-unfolding mechanism in order to exchange, are those from beta2, beta3, and beta4, the central strands of the beta-sheet, which constitute the main element of the core of the protein. The free energies obtained from exchange measurements of protons belonging to the alpha-helices are lower than those derived from GdmCl denaturation studies, indicating that those protons exchange by local-unfolding mechanisms.
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{{ABSTRACT_PUBMED_11735407}}
==About this Structure==
==About this Structure==
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1GL8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GL8 OCA].
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1GL8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GL8 OCA].
==Reference==
==Reference==
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[[Category: Electron transport]]
[[Category: Electron transport]]
[[Category: Redox-active center]]
[[Category: Redox-active center]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:43:05 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:28:28 2008''

Revision as of 02:28, 1 July 2008

Image:1gl8.png

Template:STRUCTURE 1gl8

SOLUTION STRUCTURE OF THIOREDOXIN M FROM SPINACH, OXIDIZED FORM

Template:ABSTRACT PUBMED 11735407

About this Structure

1GL8 is a Single protein structure of sequence from Spinacia oleracea. Full experimental information is available from OCA.

Reference

Three-dimensional solution structure and stability of thioredoxin m from spinach., Neira JL, Gonzalez C, Toiron C, de Prat-Gay G, Rico M, Biochemistry. 2001 Dec 18;40(50):15246-56. PMID:11735407

Page seeded by OCA on Tue Jul 1 05:28:28 2008

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