1e6l
From Proteopedia
(New page: 200px<br /><applet load="1e6l" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e6l, resolution 1.9Å" /> '''TWO-COMPONENT SIGNAL ...) |
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| - | [[Image:1e6l.gif|left|200px]]<br /><applet load="1e6l" size=" | + | [[Image:1e6l.gif|left|200px]]<br /><applet load="1e6l" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1e6l, resolution 1.9Å" /> | caption="1e6l, resolution 1.9Å" /> | ||
'''TWO-COMPONENT SIGNAL TRANSDUCTION SYSTEM D13A MUTANT OF CHEY'''<br /> | '''TWO-COMPONENT SIGNAL TRANSDUCTION SYSTEM D13A MUTANT OF CHEY'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The signal transduction protein CheY displays an alpha/beta-parallel | + | The signal transduction protein CheY displays an alpha/beta-parallel polypeptide folding, including a highly unstable helix alpha4 and a strongly charged active site. Helix alpha4 has been shown to adopt various positions and conformations in different crystal structures, suggesting that it is a mobile segment. Furthermore, the instability of this helix is believed to have functional significance because it is involved in protein-protein contacts with the transmitter protein kinase CheA, the target protein FliM and the phosphatase CheZ. The active site of CheY comprises a cluster of three aspartic acid residues and a lysine residue, all of which participate in the binding of the Mg(2+) needed for the protein activation. Two steps were followed to study the activation mechanism of CheY upon phosphorylation: first, we independently substituted the three aspartic acid residues in the active site with alanine; second, several mutations were designed in helix alpha 4, both to increase its level of stability and to improve its packing against the protein core. The structural and thermodynamic analysis of these mutant proteins provides further evidence of the connection between the active-site area and helix alpha 4, and helps to understand how small movements at the active site are transmitted and amplified to the protein surface. |
==About this Structure== | ==About this Structure== | ||
| - | 1E6L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | + | 1E6L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E6L OCA]. |
==Reference== | ==Reference== | ||
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[[Category: two-component signal transduction system]] | [[Category: two-component signal transduction system]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:24:25 2008'' |
Revision as of 10:24, 21 February 2008
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TWO-COMPONENT SIGNAL TRANSDUCTION SYSTEM D13A MUTANT OF CHEY
Overview
The signal transduction protein CheY displays an alpha/beta-parallel polypeptide folding, including a highly unstable helix alpha4 and a strongly charged active site. Helix alpha4 has been shown to adopt various positions and conformations in different crystal structures, suggesting that it is a mobile segment. Furthermore, the instability of this helix is believed to have functional significance because it is involved in protein-protein contacts with the transmitter protein kinase CheA, the target protein FliM and the phosphatase CheZ. The active site of CheY comprises a cluster of three aspartic acid residues and a lysine residue, all of which participate in the binding of the Mg(2+) needed for the protein activation. Two steps were followed to study the activation mechanism of CheY upon phosphorylation: first, we independently substituted the three aspartic acid residues in the active site with alanine; second, several mutations were designed in helix alpha 4, both to increase its level of stability and to improve its packing against the protein core. The structural and thermodynamic analysis of these mutant proteins provides further evidence of the connection between the active-site area and helix alpha 4, and helps to understand how small movements at the active site are transmitted and amplified to the protein surface.
About this Structure
1E6L is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Towards understanding a molecular switch mechanism: thermodynamic and crystallographic studies of the signal transduction protein CheY., Sola M, Lopez-Hernandez E, Cronet P, Lacroix E, Serrano L, Coll M, Parraga A, J Mol Biol. 2000 Oct 20;303(2):213-25. PMID:11023787
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