Crystallization and preliminary X-ray diffraction studies of alpha-amylase from the antarctic psychrophile Alteromonas haloplanctis A23.
A cold-active alpha-amylase was purified from culture supernatants of the antarctic psychrophile Alteromonas haloplanctis A23 grown at 4 degrees C. In order to contribute to the understanding of the molecular basis of cold adaptations, crystallographic studies of this cold-adapted enzyme have been initiated because a three-dimensional structure of a mesophilic counterpart, pig pancreatic alpha-amylase, already exists. alpha-Amylase from A. haloplanctis, which shares 53% sequence identity with pig pancreatic alpha-amylase, has been crystallized and data to 1.85 A have been collected. The space group is found to be C222(1) with a = 71.40 A, b = 138.88 A, and c = 115.66 A. Until now, a three-dimensional structure of a psychrophilic enzyme is lacking.
Laboratoire d'Architecture et Fonction des Macromolécules Biologiques, UPR9039, Institut de Biologie Structurale et Microbiologie, IFRI, CNRS, Marseille, France.
N
N
Aghajari
G
G
Feller
C
C
Gerday
R
R
Haser
D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification; D003080:Cold Temperature; D003460:Crystallization; D018360:Crystallography, X-Ray; D006090:Gram-Negative Bacteria / Q000201:enzymology*; D011487:Protein Conformation; D000516:alpha-Amylases / Q000737:chemistry* / Q000302:isolation & purification
D001426:Bacterial Proteins; D000516:alpha-Amylases