"Cold-spots" in protein cold adaptation: Insights from normalized atomic displacement parameters (-factors)

Alessandro Siglioccolo (1) , Raffaele Gerace (1) , Stefano Pascarella (1, 2)

1 Department of Biochemical Sciences "Rossi Fanelli"
2 UNIROMA - Università degli Studi di Roma "La Sapienza" = Sapienza University [Rome]

Many analyses published in the last decade suggest that enzymes isolated from cold-adapted organisms are characterized by a higher flexibility of their molecular structure. Recently, it has been argued that all cold-adapted enzymes with catalytic efficiency greater than that of their mesophilic counterparts display local flexibility or rigidity that are likely to cooperate, each acting on specific areas of the enzyme structure. Here we report an analysis of the normalized thermal -factor distributions in psychrophilic proteins compared with those of their mesophilic and thermophilic counterparts with the aim to detect statistically significant local variations of relative backbone flexibility possibly linked to cold adaptation. We utilized a strategy based mainly on intra-family comparison of local distribution of normalized -factors. After careful statistical treatment of data, the picture emerging from our results suggests that the distribution of the flexibility in psychrophilic enzymes is locally more heterogeneous than in their respective mesophilic homologues.

Mots clés: -factor; local flexibility; cold adaptation; psychrophiles; catalysis

Domaines: Chimie-Physique [physics.chem-ph]

Alessandro Siglioccolo, Raffaele Gerace, Stefano Pascarella. "Cold-spots" in protein cold adaptation: Insights from normalized atomic displacement parameters (-factors). Biophysical Chemistry, 2010, 153 (1), pp.104. ⟨10.1016/j.bpc.2010.10.009⟩. ⟨hal-00702309⟩