%A Divya Kapoor
%A Vijay Kumar
%A Sanjeev Kumar Chandrayan
%A Shubbir Ahmed
%A Swati Sharma
%A Manish Datt
%A Balvinder Singh
%A Subramanian Karthikeyan
%A Purnananda Guptasarma
%O Copyright of this article belongs to Elsevier Science.
%J Biochimica et biophysica acta
%T Replacement of the active surface of a thermophile protein by that of a homologous mesophile protein through structure-guided 'protein surface grafting'.
%X Using several tens of rationally-selected substitutions, insertions and deletions of predominantly non-contiguous residues, we have remodeled the solvent-exposed face of a beta sheet functioning as the substrate-binding and catalytically-active groove of a thermophile cellulase (Rhodothermus marinus Cel12A) to cause it to resemble, both in its structure and function, the equivalent groove of a mesophile homolog (Trichoderma reesei Cel12A). The engineered protein, a mesoactive-thermostable cellulase (MT Cel12A) displays the temperature of optimal function of its mesophile ancestor and the temperature of melting of its thermophile ancestor, suggesting that such 'grafting' of a mesophile-derived surface onto a thermophile-derived structural scaffold can potentially help generate novel enzymes that recombine structural and functional features of homologous proteins sourced from different domains of life.
%N 11
%P 1771-6
%V 1784
%D 2008
%I Elsevier Science
%L open588