1myl
From Proteopedia
(New page: 200px<br /><applet load="1myl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1myl, resolution 2.4Å" /> '''SUBSTITUTING HYDROPHO...) |
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| - | [[Image:1myl.gif|left|200px]]<br /><applet load="1myl" size=" | + | [[Image:1myl.gif|left|200px]]<br /><applet load="1myl" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1myl, resolution 2.4Å" /> | caption="1myl, resolution 2.4Å" /> | ||
'''SUBSTITUTING HYDROPHOBIC RESIDUES FOR A BURIED SALT BRIDGE ENHANCES PROTEIN STABILITY BUT DOES NOT REDUCE CONFORMATIONAL SPECIFICITY'''<br /> | '''SUBSTITUTING HYDROPHOBIC RESIDUES FOR A BURIED SALT BRIDGE ENHANCES PROTEIN STABILITY BUT DOES NOT REDUCE CONFORMATIONAL SPECIFICITY'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The side chains of Arg 31, Glu 36 and Arg 40 in Arc repressor form a | + | The side chains of Arg 31, Glu 36 and Arg 40 in Arc repressor form a buried salt-bridge triad. The entire salt-bridge network can be replaced by hydrophobic residues in combinatorial randomization experiments resulting in active mutants that are significantly more stable than wild type. The crystal structure of one mutant reveals that the mutant side chains pack against each other in an otherwise wild-type fold. Thus, simple hydrophobic interactions provide more stabilizing energy than the buried salt bridge and confer comparable conformational specificity. |
==About this Structure== | ==About this Structure== | ||
| - | 1MYL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_phage_py54 Yersinia phage py54]. Full crystallographic information is available from [http:// | + | 1MYL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_phage_py54 Yersinia phage py54]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MYL OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Yersinia phage py54]] | [[Category: Yersinia phage py54]] | ||
| - | [[Category: Sauer, R | + | [[Category: Sauer, R T.]] |
| - | [[Category: Schildbach, J | + | [[Category: Schildbach, J F.]] |
| - | [[Category: Waldburger, C | + | [[Category: Waldburger, C D.]] |
[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:00:23 2008'' |
Revision as of 12:00, 21 February 2008
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SUBSTITUTING HYDROPHOBIC RESIDUES FOR A BURIED SALT BRIDGE ENHANCES PROTEIN STABILITY BUT DOES NOT REDUCE CONFORMATIONAL SPECIFICITY
Overview
The side chains of Arg 31, Glu 36 and Arg 40 in Arc repressor form a buried salt-bridge triad. The entire salt-bridge network can be replaced by hydrophobic residues in combinatorial randomization experiments resulting in active mutants that are significantly more stable than wild type. The crystal structure of one mutant reveals that the mutant side chains pack against each other in an otherwise wild-type fold. Thus, simple hydrophobic interactions provide more stabilizing energy than the buried salt bridge and confer comparable conformational specificity.
About this Structure
1MYL is a Single protein structure of sequence from Yersinia phage py54. Full crystallographic information is available from OCA.
Reference
Are buried salt bridges important for protein stability and conformational specificity?, Waldburger CD, Schildbach JF, Sauer RT, Nat Struct Biol. 1995 Feb;2(2):122-8. PMID:7749916
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