TAILIEUCHUNG - Báo cáo khoa học: Creation of a new eye lens crystallin (Gambeta) through structure-guided mutagenic grafting of the surface of bB2 crystallin onto the hydrophobic core of cB crystallin

The degree of conservation of three-dimensional folds in protein superfami-lies is greater than that of amino acid sequences. Therefore, very different groups of residues (and schemes of residue packing) can be found displayed upon similar structural scaffolds. | Creation of a new eye lens crystallin Gambeta through structure-guided mutagenic grafting of the surface of bB2 crystallin onto the hydrophobic core of cB crystallin Divya Kapoor1 Balvinder Singh2 Karthikeyan Subramanian1 and Purnananda Guptasarma1 1 Division of Protein Science Engineering Institute of MicrobialTechnology Chandigarh 160 036 Councilof Scientific Industrial Research New Delhi India 2 Division of Bioinformatics Institute of MicrobialTechnology Chandigarh 160 036 Councilof Scientific IndustrialResearch New Delhi India Keywords beta sheet remodeling lens structural proteins protein engineering protein folding and stability protein surface grafting Correspondence P. Guptasarma Division of Protein Science Engineering Institute of Microbial Technology Chandigarh 160 036 Councilof Scientific IndustrialResearch New Delhi India Fax 91 172 2690585 Tel 91 172 2636680 ext. 3301 E-mail pg@ Received 14 February 2009 revised 2 April 2009 accepted 14 April 2009 doi The degree of conservation of three-dimensional folds in protein superfamilies is greater than that of amino acid sequences. Therefore very different groups of residues and schemes of residue packing can be found displayed upon similar structural scaffolds. We have previously demonstrated the workability of a protein engineering-based method for rational mixing of the interior features of an all-beta enzyme with the substrate-binding and catalytic surface features of another enzyme whose sequence is not similar but which is structurally homologous to the first enzyme. Here we extend this method to whole-protein surfaces and interiors. We show how two allbeta Greek key proteins bB2 crystallin and yB crystallin can be recombined to produce a new protein through rational transplantation of the entire surface of bB2 crystallin upon the structure of yB crystallin without altering the latter s interior. This new protein Gambeta consists of 61 residues possessing the

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