Comparative Protein Modeling, Prediction of Conserved Residue and Active Sites in Cold Resistant Protein Isolated from CRPF1, A Cold Tolerant Mutant of Pseudomonas fluorescens.

Proteins interacting with the biological information
molecules DNA and RNA play important cellular
roles in all organisms. One widespread super family of
proteins implicated in such function(s) is cold shock protein
(CSP) that contains the cold shock domain (CSD). This
work is planned to study the three-dimensional structure,
conserved residues, and different active sites in the structure
of cold resistant protein (CRP) from CRPF1, cold
tolerant mutant of Pseudomonas fluorescence by comparative
homology modeling. Here we tried to identify crucial
residues that are involved in active sites or functional sites
of the protein. The study reveals that CRP represent the
prototype of the CSD and share a highly similar overall
fold consisting of five antiparallel b-sheets forming a
b-barrel structure with surface exposed aromatic and basic
residues that were responsible for nucleic acid binding
properties of variable binding affinities and sequence
selectivity and harbors the nucleic acid binding motifs
RNP1 and RNP2 that is highly conserved in CSP family.