Zinc, a novel structural element found in the family of bacterial adenylate kinases.
The adk gene from Bacillus stearothermophilus was cloned and overexpressed in Escherichia coli under the control of the lac promoter. The primary structure of B. stearothermophilus adenylate kinase exhibited 76% identity with the enzyme from Bacillus subtilis, 60% identity with the enzyme from Lactococcus lactis, and 42% identity with the enzyme from E. coli. The most striking property of the adenylate kinase from B. stearothermophilus is the presence of a structural zinc atom bound to four cysteines in a zinc finger-like fashion. The ability to coordinate zinc is predicted also for a number of other isoforms of bacterial adenylate kinases. Furthermore, the tightly bound metal ion contributes to the high thermodynamic stability of adenylate kinase from B. stearothermophilus.
Glaser
P
P
Unité de Régulation de l'Expression Génétique, Institut Pasteur, Paris, France.
Presecan
E
E
Delepierre
M
M
Surewicz
W K
WK
Mantsch
H H
HH
Bârzu
O
O
Gilles
A M
AM
D000263:Adenylate Kinase / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D001483:Base Sequence; D003001:Cloning, Molecular; D004795:Enzyme Stability; D005798:Genes, Bacterial; D005822:Genetic Vectors; D001411:Geobacillus stearothermophilus / Q000737:chemistry* / Q000201:enzymology / Q000235:genetics; D007700:Kinetics; D008969:Molecular Sequence Data; D005810:Multigene Family; D011485:Protein Binding; D013329:Structure-Activity Relationship; D013816:Thermodynamics; D015032:Zinc / Q000737:chemistry*
D001426:Bacterial Proteins; D000263:Adenylate Kinase; D015032:Zinc