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1m7t

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{{STRUCTURE_1m7t| PDB=1m7t | SCENE= }}
{{STRUCTURE_1m7t| PDB=1m7t | SCENE= }}
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'''Solution Structure and Dynamics of the Human-Escherichia coli Thioredoxin Chimera: Insights into Thermodynamic Stability'''
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===Solution Structure and Dynamics of the Human-Escherichia coli Thioredoxin Chimera: Insights into Thermodynamic Stability===
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==Overview==
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We have determined the high-resolution solution structure of the oxidized form of a chimeric human and Escherichia coli thioredoxin (TRX(HE)) by NMR. The overall structure is well-defined with a rms difference for the backbone atoms of 0.27 +/- 0.06 A. The topology of the protein is identical to those of the human and E. coli parent proteins, consisting of a central five-stranded beta-sheet surrounded by four alpha-helices. Analysis of the interfaces between the two domains derived from the human and E. coli sequences reveals that the general hydrophobic packing is unaltered and only subtle changes in the details of side chain interactions are observed. The packing of helix alpha(4) with helix alpha(2) across the hybrid interface is less optimal than in the parent molecules, and electrostatic interactions between polar side chains are missing. In particular, lysine-glutamate salt bridges between residues on helices alpha(2) and alpha(4), which were observed in both human and E. coli proteins, are not present in the chimeric protein. The origin of the known reduced thermodynamic stability of TRX(HE) was probed by mutagenesis on the basis of these structural findings. Two mutants of TRX(HE), S44D and S44E, were created, and their thermal and chemical stabilities were examined. Improved stability toward chaotropic agents was observed for both mutants, but no increase in the denaturation temperature was seen compared to that of TRX(HE). In addition to the structural analysis, the backbone dynamics of TRX(HE) were investigated by (15)N NMR relaxation measurements. Analysis using the model free approach reveals that the protein is fairly rigid with an average S(2) of 0.88. Increased mobility is primarily present in two external loop regions comprising residues 72-74 and 92-94 that contain glycine and proline residues.
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(as it appears on PubMed at http://www.pubmed.gov), where 12135359 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12135359}}
==About this Structure==
==About this Structure==
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1M7T is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens_and_escherichia_coli Homo sapiens and escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M7T OCA].
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1M7T is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens_and_escherichia_coli Homo sapiens and escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M7T OCA].
==Reference==
==Reference==
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[[Category: Human]]
[[Category: Human]]
[[Category: Stability]]
[[Category: Stability]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:44:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 23:24:01 2008''

Revision as of 20:24, 2 July 2008

Image:1m7t.png

Template:STRUCTURE 1m7t

Solution Structure and Dynamics of the Human-Escherichia coli Thioredoxin Chimera: Insights into Thermodynamic Stability

Template:ABSTRACT PUBMED 12135359

About this Structure

1M7T is a Single protein structure of sequence from Homo sapiens and escherichia coli. Full experimental information is available from OCA.

Reference

Solution structure and dynamics of the human-Escherichia coli thioredoxin chimera: insights into thermodynamic stability., Dangi B, Dobrodumov AV, Louis JM, Gronenborn AM, Biochemistry. 2002 Jul 30;41(30):9376-88. PMID:12135359

Page seeded by OCA on Wed Jul 2 23:24:01 2008

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