1gto
From Proteopedia
(New page: 200px<br /><applet load="1gto" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gto, resolution 1.82Å" /> '''HIGH RESOLUTION STRU...) |
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| - | [[Image:1gto.gif|left|200px]]<br /><applet load="1gto" size=" | + | [[Image:1gto.gif|left|200px]]<br /><applet load="1gto" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1gto, resolution 1.82Å" /> | caption="1gto, resolution 1.82Å" /> | ||
'''HIGH RESOLUTION STRUCTURE OF A HYPERSTABLE HELICAL BUNDLE PROTEIN MUTANT'''<br /> | '''HIGH RESOLUTION STRUCTURE OF A HYPERSTABLE HELICAL BUNDLE PROTEIN MUTANT'''<br /> | ||
==Overview== | ==Overview== | ||
| - | A surface turn position in a four-helix bundle protein, Rop, was selected | + | A surface turn position in a four-helix bundle protein, Rop, was selected to investigate the role of turns in protein structure and stability. Although all twenty amino acids can be substituted at this position to generate a correctly folded protein, they produce an unusually large range of thermodynamic stabilities. Moreover, the majority of substitutions give rise to proteins with enhanced thermal stability compared to that of the wild type. By introducing the same twenty mutations at this position, but in a simplified context, we were able to deconvolute intrinsic preferences from local environmental effects. The intrinsic preferences can be explained on the basis of preferred backbone dihedral angles, but local environmental context can significantly modify these effects. |
==About this Structure== | ==About this Structure== | ||
| - | 1GTO 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:// | + | 1GTO 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=1GTO OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Agrawal, V.]] | [[Category: Agrawal, V.]] | ||
| - | [[Category: Brunger, A | + | [[Category: Brunger, A T.]] |
[[Category: Predki, P.]] | [[Category: Predki, P.]] | ||
[[Category: Regan, L.]] | [[Category: Regan, L.]] | ||
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[[Category: turn]] | [[Category: turn]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:54:03 2008'' |
Revision as of 10:54, 21 February 2008
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HIGH RESOLUTION STRUCTURE OF A HYPERSTABLE HELICAL BUNDLE PROTEIN MUTANT
Overview
A surface turn position in a four-helix bundle protein, Rop, was selected to investigate the role of turns in protein structure and stability. Although all twenty amino acids can be substituted at this position to generate a correctly folded protein, they produce an unusually large range of thermodynamic stabilities. Moreover, the majority of substitutions give rise to proteins with enhanced thermal stability compared to that of the wild type. By introducing the same twenty mutations at this position, but in a simplified context, we were able to deconvolute intrinsic preferences from local environmental effects. The intrinsic preferences can be explained on the basis of preferred backbone dihedral angles, but local environmental context can significantly modify these effects.
About this Structure
1GTO is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Amino-acid substitutions in a surface turn modulate protein stability., Predki PF, Agrawal V, Brunger AT, Regan L, Nat Struct Biol. 1996 Jan;3(1):54-8. PMID:8548455
Page seeded by OCA on Thu Feb 21 12:54:03 2008
