1quw
From Proteopedia
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| - | [[Image:1quw.jpg|left|200px]] | + | [[Image:1quw.jpg|left|200px]] |
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| - | '''SOLUTION STRUCTURE OF THE THIOREDOXIN FROM BACILLUS ACIDOCALDARIUS''' | + | {{Structure |
| + | |PDB= 1quw |SIZE=350|CAPTION= <scene name='initialview01'>1quw</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''SOLUTION STRUCTURE OF THE THIOREDOXIN FROM BACILLUS ACIDOCALDARIUS''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1QUW is a [ | + | 1QUW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Alicyclobacillus_acidocaldarius Alicyclobacillus acidocaldarius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QUW OCA]. |
==Reference== | ==Reference== | ||
| - | NMR solution structure of a novel thioredoxin from Bacillus acidocaldarius possible determinants of protein stability., Nicastro G, De Chiara C, Pedone E, Tato M, Rossi M, Bartolucci S, Eur J Biochem. 2000 Jan;267(2):403-13. PMID:[http:// | + | NMR solution structure of a novel thioredoxin from Bacillus acidocaldarius possible determinants of protein stability., Nicastro G, De Chiara C, Pedone E, Tato M, Rossi M, Bartolucci S, Eur J Biochem. 2000 Jan;267(2):403-13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10632710 10632710] |
[[Category: Alicyclobacillus acidocaldarius]] | [[Category: Alicyclobacillus acidocaldarius]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: thiol-disulfide]] | [[Category: thiol-disulfide]] | ||
| - | ''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 13:43:07 2008'' |
Revision as of 11:43, 20 March 2008
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SOLUTION STRUCTURE OF THE THIOREDOXIN FROM BACILLUS ACIDOCALDARIUS
Overview
The thioredoxin (Trx) from Bacillus acidocaldarius (BacTrx), an eubacterium growing optimally at 333 K, is the first Trx described to date from a moderate thermophilic source. To understand the molecular basis of its thermostability, the three-dimensional structure in the oxidized form was determined by NMR methods. A total of 2276 1H-NMR derived distance constraints along with 23 hydrogen-bonds, 72 phi and 27 chi1 torsion angle restraints, were used in a protocol employing simulated annealing followed by restrained molecular dynamics and restrained energy minimization. BacTrx consists of a well-defined core region of five strands of beta-sheet, surrounded by four exposed alpha-helices, features shared by other members of the thioredoxin family. The BacTrx 3D structure was compared with the Escherichia coli Trx (EcTrx) determined by X-ray crystallographic diffraction, and a number of structural differences were observed that may contribute to its thermostabilty. The results of structural analysis indicated that protein stability is due to cumulative effects, the main factor being an increased number of ionic interactions cross-linking different secondary structural elements and clamping the C-terminal alpha-helix to the core of the protein.
About this Structure
1QUW is a Single protein structure of sequence from Alicyclobacillus acidocaldarius. Full crystallographic information is available from OCA.
Reference
NMR solution structure of a novel thioredoxin from Bacillus acidocaldarius possible determinants of protein stability., Nicastro G, De Chiara C, Pedone E, Tato M, Rossi M, Bartolucci S, Eur J Biochem. 2000 Jan;267(2):403-13. PMID:10632710
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