Structural features in the model of a thermostable and stress-resistant protein, SP1 from aspen.
A three dimensional theoretical model of SP1 (stable protein 1), which is resistant to high temperature and biotic-stresses, is presented here. The model was generated by the application of homology modeling technique. The conformational rigidity imparted to the fold by the presence of hydrogen-bonded, C5, C7, C10 and C13 structures in the loop regions, multiple aromatic--aromatic interactions at the protein interior and on the surface, in addition to salt-links and hydrogen-bonds are primarily the major factors, responsible for the increased stability of protein. The putative protein family is characterized by motifs, E-x(0,1)-L-x-[AEGQS] and V-x(2,3)-L-x-[ADEGST] and the active site in the tertiary structure is formed by conserved aromatic and isoleucine clusters.
Rathore
Ravindranath S
RS
Department of Physics, Indian Institute of Science, Bangalore 560 012, India. newdrugdesign@yahoo.com
Narasimhamurthy
T
T
D000595:Amino Acid Sequence; D008958:Models, Molecular; D008969:Molecular Sequence Data; D032107:Populus / Q000737:chemistry*; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*
D011506:Proteins