2h6z
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene> | |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.] | + | |ACTIVITY= <span class='plainlinks'>[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.] </span> |
|GENE= trxA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= trxA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2trx|2TRX]], [[1zzy|1ZZY]], [[2fch|2FCH]], [[2fd3|2FD3]], [[2h6x|2H6X]], [[2h6y|2H6Y]], [[2h70|2H70]], [[2h71|2H71]], [[2h72|2H72]], [[2h73|2H73]], [[2h74|2H74]], [[2h75|2H75]], [[2h76|2H76]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2h6z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h6z OCA], [http://www.ebi.ac.uk/pdbsum/2h6z PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2h6z RCSB]</span> | ||
}} | }} | ||
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[[Category: Ibarra-Molero, B.]] | [[Category: Ibarra-Molero, B.]] | ||
[[Category: Sanchez-Ruiz, J M.]] | [[Category: Sanchez-Ruiz, J M.]] | ||
| - | [[Category: MPD]] | ||
[[Category: alpha beta]] | [[Category: alpha beta]] | ||
[[Category: electron transport]] | [[Category: electron transport]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:26:21 2008'' |
Revision as of 00:26, 31 March 2008
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| , resolution 2.250Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | trxA (Escherichia coli) | ||||||
| Activity: | Lyase, with EC number 4.7.1.4. | ||||||
| Related: | 2TRX, 1ZZY, 2FCH, 2FD3, 2H6X, 2H6Y, 2H70, 2H71, 2H72, 2H73, 2H74, 2H75, 2H76
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Thioredoxin Mutant E44D in Hexagonal (p61) Space Group
Overview
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 Structure
2H6Z is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
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:16100262
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