1gto
From Proteopedia
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| - | [[Image:1gto.gif|left|200px]] | + | [[Image:1gto.gif|left|200px]] |
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| - | '''HIGH RESOLUTION STRUCTURE OF A HYPERSTABLE HELICAL BUNDLE PROTEIN MUTANT''' | + | {{Structure |
| + | |PDB= 1gto |SIZE=350|CAPTION= <scene name='initialview01'>1gto</scene>, resolution 1.82Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''HIGH RESOLUTION STRUCTURE OF A HYPERSTABLE HELICAL BUNDLE PROTEIN MUTANT''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1GTO is a [ | + | 1GTO is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8548455 8548455] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Predki, P.]] | [[Category: Predki, P.]] | ||
[[Category: Regan, L.]] | [[Category: Regan, L.]] | ||
| - | [[Category: crystal | + | [[Category: crystal contact]] |
[[Category: helix packing]] | [[Category: helix packing]] | ||
[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
[[Category: turn]] | [[Category: turn]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:27:44 2008'' |
Revision as of 09:27, 20 March 2008
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| , resolution 1.82Å | |||||||
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| 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
Page seeded by OCA on Thu Mar 20 11:27:44 2008
