Comparative Protein Modeling, Prediction of Conserved Residue and Active Sites in Cold Resistant Protein Isolated from CRPF1, A Cold Tolerant Mutant of Pseudomonas fluorescens |
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Authors: | Mahejibin Khan Amit Kumar Reeta Goel |
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Institution: | (1) Food Microbiology Department, CFTRI, Mysore, India;(2) Amity Institute of Biotechnology, Amity University Rajasthan Campus, Jaipur, India;(3) Department of Microbiology, GBPAUT, Pantnagar, 263145, Uttarakhand, India |
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Abstract: | 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 β-sheets forming a β-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. |
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Keywords: | |
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