1cx6

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(New page: 200px<br /><applet load="1cx6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cx6, resolution 2.01&Aring;" /> '''T4 LYSOZYME SUBSTITU...)
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[[Image:1cx6.gif|left|200px]]<br /><applet load="1cx6" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1cx6.gif|left|200px]]<br /><applet load="1cx6" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1cx6, resolution 2.01&Aring;" />
caption="1cx6, resolution 2.01&Aring;" />
'''T4 LYSOZYME SUBSTITUTED WITH SELENOMETHIONINE'''<br />
'''T4 LYSOZYME SUBSTITUTED WITH SELENOMETHIONINE'''<br />
==Overview==
==Overview==
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The availability of a series of phage T4 lysozymes with up to 14, methionine residues incorporated within the protein has made it possible, to systematically compare the effect on protein stability of, selenomethionine relative to methionine. Wild-type lysozyme contains two, fully buried methionine residues plus three more on the surface. The, substitution of these methionine residues with selenomethionine slightly, stabilizes the protein. As more and more methionine residues are, substituted into the protein, there is a progressive loss of stability., This is, however, increasingly offset in the selenomethionine variants, ultimately resulting in a differential increase in melting temperature of, about 7 degrees C. This increase, corresponding to about 0.25 kcal/mol per, substitution, is in reasonable agreement with the difference in the, solvent transfer free energy between the two amino acids.
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The availability of a series of phage T4 lysozymes with up to 14 methionine residues incorporated within the protein has made it possible to systematically compare the effect on protein stability of selenomethionine relative to methionine. Wild-type lysozyme contains two fully buried methionine residues plus three more on the surface. The substitution of these methionine residues with selenomethionine slightly stabilizes the protein. As more and more methionine residues are substituted into the protein, there is a progressive loss of stability. This is, however, increasingly offset in the selenomethionine variants, ultimately resulting in a differential increase in melting temperature of about 7 degrees C. This increase, corresponding to about 0.25 kcal/mol per substitution, is in reasonable agreement with the difference in the solvent transfer free energy between the two amino acids.
==About this Structure==
==About this Structure==
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1CX6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4] with CL and HED as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CX6 OCA].
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1CX6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4] with <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=HED:'>HED</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CX6 OCA].
==Reference==
==Reference==
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[[Category: Lysozyme]]
[[Category: Lysozyme]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Baase, W.A.]]
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[[Category: Baase, W A.]]
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[[Category: Gassner, N.C.]]
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[[Category: Gassner, N C.]]
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[[Category: Matthews, B.W.]]
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[[Category: Matthews, B W.]]
[[Category: CL]]
[[Category: CL]]
[[Category: HED]]
[[Category: HED]]
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[[Category: t4 lysozyme]]
[[Category: t4 lysozyme]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:49:14 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:10:40 2008''

Revision as of 10:10, 21 February 2008


1cx6, resolution 2.01Å

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T4 LYSOZYME SUBSTITUTED WITH SELENOMETHIONINE

Overview

The availability of a series of phage T4 lysozymes with up to 14 methionine residues incorporated within the protein has made it possible to systematically compare the effect on protein stability of selenomethionine relative to methionine. Wild-type lysozyme contains two fully buried methionine residues plus three more on the surface. The substitution of these methionine residues with selenomethionine slightly stabilizes the protein. As more and more methionine residues are substituted into the protein, there is a progressive loss of stability. This is, however, increasingly offset in the selenomethionine variants, ultimately resulting in a differential increase in melting temperature of about 7 degrees C. This increase, corresponding to about 0.25 kcal/mol per substitution, is in reasonable agreement with the difference in the solvent transfer free energy between the two amino acids.

About this Structure

1CX6 is a Single protein structure of sequence from Bacteriophage t4 with and as ligands. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.

Reference

Substitution with selenomethionine can enhance the stability of methionine-rich proteins., Gassner NC, Baase WA, Hausrath AC, Matthews BW, J Mol Biol. 1999 Nov 19;294(1):17-20. PMID:10556025

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