Thermostability

Citrate synthase

The PDB code links will take you to the PDB entry with links to the publication

 
 

A comparative structural study was undertaken to establish the basis of heat and cold tolerance. Citrate synthase was used as a model enzyme, and structures were determined from organisms spanning the temperature rang eat which life is found: 0C to >100C. Factors such as networks of ion paris (shown below) and removal of internal cavities correlated with increasing temperature. This study was in collaboration with Mike Danson & David Hough at the University of Bath.

Antartic bacterium (0C)      T. acidophilum (55C)        S. solfataricus (85C)         P. furiosus (100C)

PDB codes: 1a59http://www.rcsb.org/pdb/explore.do?structureId=1A59
1o7xhttp://www.rcsb.org/pdb/explore.do?structureId=1O7X
1aj8http://www.rcsb.org/pdb/explore.do?structureId=1AJ8

Triosephosphate isomerase

Most TIMs are dimers, but in thermophilic archaea they are tetramers. The P. furiosus TIM has a smaller monomer, and achieves thermostability through shorter loops and a predominantly hydrophobic interaction of two classical dimers to form the tetramer. This study was in collaboration with Mike Danson & David Hough at the University of Bath.

PDB codes: 1hg3 (P. furiosus), http://www.rcsb.org/pdb/explore.do?structureId=1HG3
1w0m (T. tenax)http://www.rcsb.org/pdb/explore.do?structureId=1W0M