Two exposed amino acid residues confer thermostability on a cold shock protein - PubMed (original) (raw)
Comparative Study
doi: 10.1038/75151.
Affiliations
- PMID: 10802734
- DOI: 10.1038/75151
Comparative Study
Two exposed amino acid residues confer thermostability on a cold shock protein
D Perl et al. Nat Struct Biol. 2000 May.
Abstract
Thermophilic organisms produce proteins of exceptional stability. To understand protein thermostability at the molecular level we studied a pair of cold shock proteins, one of mesophilic and one of thermophilic origin, by systematic mutagenesis. Although the two proteins differ in sequence at 12 positions, two surface-exposed residues are responsible for the increase in stability of the thermophilic protein (by 15.8 kJ mol-1 at 70 degrees C). 11.5 kJ mol-1 originate from a predominantly electrostatic contribution of Arg 3 and 5.2 kJ mol-1 from hydrophobic interactions of Leu 66 at the carboxy terminus. The mesophilic protein could be converted to a highly thermostable form by changing the Glu residues at positions 3 and 66 to Arg and Leu, respectively. The variation of surface residues may thus provide a simple and powerful approach for increasing the thermostability of a protein.
Comment in
- Single surface stabilizer.
Pace CN. Pace CN. Nat Struct Biol. 2000 May;7(5):345-6. doi: 10.1038/75100. Nat Struct Biol. 2000. PMID: 10802723 No abstract available.
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