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Structural features of the Est16 model in comparison with an esterase from P. fluorescens and the Anti-Kazlauskas lipase.

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posted on 2015-07-27, 03:13 authored by Mariana Rangel Pereira, Gustavo Fernando Mercaldi, Thaís Carvalho Maester, Andrea Balan, Eliana Gertrudes de Macedo Lemos

(A) Ribbon representation of the Est16 model (green) superposed on the structures of P. fluorescens esterase (blue) and the patented lipase (patent number US20050153404) (purple) revealing the conservation of the alpha/beta fold. N is the N-terminal. (B) A detailed picture of the residues from the catalytic triad of the three enzymes showing the structural superposition. Residues are shown in the following order: Est16, Pfl (PDB code 1VA4) and Anti-Kazlauskas lipase. A comparative analysis of the domains and pockets of Est16 (C), the Anti-Kazlauskas lipase model (D) and the structure of the P. fluorescens aryl-esterase (E) are shown in the cartoon. Helices are blue, β-sheets are cyan and the residues in the active site are shown as yellow sticks. The large and small domains are delimited in the three proteins.

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