2h70: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:2h70.jpg|left|200px]] | [[Image:2h70.jpg|left|200px]] | ||
'''Crystal Structure of Thioredoxin Mutant D9E in Hexagonal (p61) Space Group''' | {{Structure | ||
|PDB= 2h70 |SIZE=350|CAPTION= <scene name='initialview01'>2h70</scene>, resolution 2.70Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Lyase Lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.7.1.4 4.7.1.4] | |||
|GENE= trxA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |||
}} | |||
'''Crystal Structure of Thioredoxin Mutant D9E in Hexagonal (p61) Space Group''' | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
2H70 is a [ | 2H70 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=2H70 OCA]. | ||
==Reference== | ==Reference== | ||
A stability pattern of protein hydrophobic mutations that reflects evolutionary structural optimization., Godoy-Ruiz R, Perez-Jimenez R, Ibarra-Molero B, Sanchez-Ruiz JM, Biophys J. 2005 Nov;89(5):3320-31. Epub 2005 Aug 12. PMID:[http:// | A stability pattern of protein hydrophobic mutations that reflects evolutionary structural optimization., Godoy-Ruiz R, Perez-Jimenez R, Ibarra-Molero B, Sanchez-Ruiz JM, Biophys J. 2005 Nov;89(5):3320-31. Epub 2005 Aug 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16100262 16100262] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Lyase]] | [[Category: Lyase]] | ||
| Line 22: | Line 31: | ||
[[Category: electron transport]] | [[Category: electron transport]] | ||
''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 17:13:33 2008'' | ||
Revision as of 18:13, 20 March 2008
| |||||||
| , resolution 2.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | trxA (Escherichia coli) | ||||||
| Activity: | Lyase, with EC number 4.7.1.4 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Thioredoxin Mutant D9E in Hexagonal (p61) Space Group
OverviewOverview
We have determined the effect of mutations involving isoleucine and valine (i.e., mutations I-->V and V-->I) on the stability of Escherichia coli thioredoxin. Despite the similarity in chemical structure (V and I differ only in a methyl group), we find that many environments are optimized to a significant extent for either V or I. We find, furthermore, that a plot of effect of hydrophobic mutations on stability versus packing density shows a strikingly simple pattern that clearly reflects evolutionary structural optimization. The existence of such patterns suggests the possibility of rationalizing (and perhaps even predicting) mutation effects on protein stability on the basis of evolutionary models. By "evolutionary model" we specifically refer in this context to a model for mutation effects on stability in which certain physical features of the mutated residue environments are evaluated from an assumption regarding how such environments have been selected during protein evolution (as opposed to a purely "physical model" in which those features would be derived from some kind of energetics analysis of the protein structural characteristics). To illustrate this novel approach and provide general guidelines for its application, we develop here a simple evolutionary model that successfully explains the effect of the I<-->V mutations on thioredoxin stability.
About this StructureAbout this Structure
2H70 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
A stability pattern of protein hydrophobic mutations that reflects evolutionary structural optimization., Godoy-Ruiz R, Perez-Jimenez R, Ibarra-Molero B, Sanchez-Ruiz JM, Biophys J. 2005 Nov;89(5):3320-31. Epub 2005 Aug 12. PMID:16100262
Page seeded by OCA on Thu Mar 20 17:13:33 2008