[en] The alpha-amylase precursor from the bacterium Pseudoalteromonas haloplanktis possesses a propeptide at the C-terminus possibly responsible for outer membrane translocation. Unlike the predicted beta-barrel of autotransporters, this C-terminal propeptide displays a noticeable alpha-helix content. It is connected to the enzyme by a disordered linker and has no significant interaction with the catalytic domain. The microcalorimetric pattern of the precursor also demonstrates that the stability of protein domains may evolve differently. (C) 2003 Elsevier B.V. All rights reserved.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Claverie, P.
Vigano, C.
Ruysschaert, J. M.
Gerday, Charles ; Université de Liège - ULiège > Services généraux (Faculté des sciences) > Relations académiques et scientifiques (Sciences)
Feller, Georges ; Université de Liège - ULiège > Département des sciences de la vie > Labo de biochimie
Language :
English
Title :
The precursor of a psychrophilic alpha-amylase: structural characterization and insights into cold adaptation
Publication date :
30 July 2003
Journal title :
Biochimica et Biophysica Acta - Proteins and Proteomics
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