1gto
From Proteopedia
| Line 29: | Line 29: | ||
[[Category: Predki, P.]] | [[Category: Predki, P.]] | ||
[[Category: Regan, L.]] | [[Category: Regan, L.]] | ||
| - | [[Category: | + | [[Category: Crystal contact]] |
| - | [[Category: | + | [[Category: Helix packing]] |
| - | [[Category: | + | [[Category: Transcription regulation]] |
| - | [[Category: | + | [[Category: Turn]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat Apr 5 18:59:26 2008'' |
Revision as of 15:59, 5 April 2008
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| , resolution 1.82Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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