2H6Z

Crystal Structure of Thioredoxin Mutant E44D in Hexagonal (p61) Space Group

Summary for 2H6Z

• Entry DOI: 10.2210/pdb2h6z/pdb
• Related: 1ZZY 2FCH 2FD3 2H6X 2H6Y 2H70 2H71 2H72 2H73 2H74 2H75 2H76 2TRX
• Descriptor: Thioredoxin, (4S)-2-METHYL-2,4-PENTANEDIOL (3 entities in total)
• Functional Keywords: alpha beta, electron transport
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 23701.24

Authors

Gavira, J.A.,Godoy-Ruiz, R.,Ibarra-Molero, B.,Sanchez-Ruiz, J.M. (deposition date: 2006-06-01, release date: 2007-05-15, Last modification date: 2024-10-16)

Primary citation

Godoy-Ruiz, R.,Perez-Jimenez, R.,Ibarra-Molero, B.,Sanchez-Ruiz, J.M.
A stability pattern of protein hydrophobic mutations that reflects evolutionary structural optimization.
Biophys.J., 89:3320-3331, 2005

PubMed Abstract: 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.

PubMed: 16100262
DOI: 10.1529/biophysj.105.067025

Experimental method

X-RAY DIFFRACTION (2.25 Å)