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Replacement of the active surface of a thermophile protein by that of a homologous mesophile protein through structure-guided 'protein surface grafting'.

DIR@IMTECH: CSIR-Institute of Microbial Technology

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Title Replacement of the active surface of a thermophile protein by that of a homologous mesophile protein through structure-guided 'protein surface grafting'.
 
Creator Kapoor, Divya
Kumar, Vijay
Chandrayan, Sanjeev Kumar
Ahmed, Shubbir
Sharma, Swati
Datt, Manish
Singh, Balvinder
Karthikeyan, Subramanian
Guptasarma, Purnananda
 
Subject QR Microbiology
 
Description 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.
 
Publisher Elsevier Science
 
Date 2008-11
 
Type Article
PeerReviewed
 
Format application/pdf
 
Identifier http://crdd.osdd.net/open/588/1/guptasarma08.16.pdf
Kapoor, Divya and Kumar, Vijay and Chandrayan, Sanjeev Kumar and Ahmed, Shubbir and Sharma, Swati and Datt, Manish and Singh, Balvinder and Karthikeyan, Subramanian and Guptasarma, Purnananda (2008) Replacement of the active surface of a thermophile protein by that of a homologous mesophile protein through structure-guided 'protein surface grafting'. Biochimica et biophysica acta, 1784 (11). pp. 1771-6. ISSN 0006-3002
 
Relation http://www.sciencedirect.com/science/article/pii/S1570963908001684
http://crdd.osdd.net/open/588/