Enzymes adapted to cold display structures comparable with those of their meso- and thermophilic homologs but are characterized by a higher catalytic efficiency at low temperatures and by thermolability at moderate temperatures. To identify the structural factors responsible of such features, we undertook a systematic comparative analysis of several structural properties in a data set consisting of 7 cold active enzymes belonging to different structural families and 28 related structures from meso/thermophiles representing most of the structural information now available. Only high-resolution and high-quality structures were considered. Properties were calculated and then compared for each pair of 3D structures displaying different temperatures of adaptation using a temperature-weighting scheme. The significance of the resulting differences was evaluated with a statistical method. Results reveal that each protein family adopts different structural strategies to adapt to low temperatures. However, some common trends are observed: the number of ion pairs, the side-chain contribution to the exposed surface, and the apolar fraction of the buried surface show a consistent decrease with decreasing optimal temperatures.

Comparative structural analysis of psychrophilic and meso- and thermophilic enzymes / Gianese, Giulio; Bossa, Francesco; Pascarella, Stefano. - In: PROTEINS. - ISSN 0887-3585. - STAMPA. - 47:2(2002), pp. 236-249. [10.1002/prot.10084]

Comparative structural analysis of psychrophilic and meso- and thermophilic enzymes

GIANESE, Giulio;BOSSA, Francesco;PASCARELLA, Stefano
2002

Abstract

Enzymes adapted to cold display structures comparable with those of their meso- and thermophilic homologs but are characterized by a higher catalytic efficiency at low temperatures and by thermolability at moderate temperatures. To identify the structural factors responsible of such features, we undertook a systematic comparative analysis of several structural properties in a data set consisting of 7 cold active enzymes belonging to different structural families and 28 related structures from meso/thermophiles representing most of the structural information now available. Only high-resolution and high-quality structures were considered. Properties were calculated and then compared for each pair of 3D structures displaying different temperatures of adaptation using a temperature-weighting scheme. The significance of the resulting differences was evaluated with a statistical method. Results reveal that each protein family adopts different structural strategies to adapt to low temperatures. However, some common trends are observed: the number of ion pairs, the side-chain contribution to the exposed surface, and the apolar fraction of the buried surface show a consistent decrease with decreasing optimal temperatures.
2002
cold adaptation; electrostatic interactions; packing density; protein cavities; protein stability; secondary structural variations; solvation free energy; structural differences; surface properties
01 Pubblicazione su rivista::01a Articolo in rivista
Comparative structural analysis of psychrophilic and meso- and thermophilic enzymes / Gianese, Giulio; Bossa, Francesco; Pascarella, Stefano. - In: PROTEINS. - ISSN 0887-3585. - STAMPA. - 47:2(2002), pp. 236-249. [10.1002/prot.10084]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/251834
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