Thermostability in rubredoxin and its relationship to mechanical rigidity.
The source of increased stability in proteins from organisms that thrive in extreme thermal environments is not well understood. Previous experimental and theoretical studies have suggested many different features possibly responsible for such thermostability. Many of these thermostabilizing mechanisms can be accounted for in terms of structural rigidity. Thus a plausible hypothesis accounting for this remarkable stability in thermophilic enzymes states that these enzymes have enhanced conformational rigidity at temperatures below their native, functioning temperature. Experimental evidence exists to both support and contradict this supposition. We computationally investigate the relationship between thermostability and rigidity using rubredoxin as a case study. The mechanical rigidity is calculated using atomic models of homologous rubredoxin structures from the hyperthermophile Pyrococcus furiosus and mesophile Clostridium pasteurianum using the FIRST software. A global increase in structural rigidity (equivalently a decrease in flexibility) corresponds to an increase in thermostability. Locally, rigidity differences (between mesophilic and thermophilic structures) agree with differences in protection factors.
Rader
A J
AJ
Department of Physics and Center for Mathematical Biosciences, Indiana University-Purdue University at Indianapolis, Indianapolis, IN, USA. ajrader@iupui.edu
D019843:Archaeal Proteins / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry*; D003013:Clostridium / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding; D055550:Protein Stability; D020027:Pyrococcus furiosus / Q000737:chemistry*; D012416:Rubredoxins / Q000737:chemistry*; D012984:Software; D013696:Temperature
D019843:Archaeal Proteins; D001426:Bacterial Proteins; D012416:Rubredoxins