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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
1991-4-17
pubmed:abstractText
A truncated, 541-residue-long, Bacillus anthracis adenylate cyclase was expressed in Escherichia coli. The purified protein (CYA 62) exhibited catalytic and CaM-binding properties identical with those of the wild-type enzyme secreted by B. anthracis. The analysis of the secondary structure of the CYA 62 protein by Fourier transform infrared spectroscopy and circular dichroism revealed the dominance of beta-type structure. The protein shows a relatively low thermal stability with the midpoint denaturation temperature at 45 degrees C. A catalytically inactive variant of CYA 62 in which Gln substituted for Lys-346 (CYA 62 K346Q) was comparatively analyzed for its secondary structure and thermal stability, as well as ligand-binding properties with fluorescent derivatives of ATP and calmodulin. The K346Q variant of CYA 62 has a similar secondary structure and comparable calmodulin binding properties to those of the parent protein and exhibits only slightly reduced thermal stability (the apparent midpoint denaturation temperature is at 43 degrees C). Despite these similarities, the binding of 3'-anthraniloyl-2'-deoxy-ATP (a fluorescent ATP analogue) to the modified protein is severely impaired, from which we conclude that the prime function of Lys-346 in the wild-type enzyme from B. anthracis is to ensure tight binding of the nucleotide substrate to the active site.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
12
pubmed:volume
30
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2619-24
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:1900429-Adenylate Cyclase, pubmed-meshheading:1900429-Amino Acid Sequence, pubmed-meshheading:1900429-Bacillus anthracis, pubmed-meshheading:1900429-Calmodulin, pubmed-meshheading:1900429-Catalysis, pubmed-meshheading:1900429-Circular Dichroism, pubmed-meshheading:1900429-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:1900429-Gene Expression Regulation, Bacterial, pubmed-meshheading:1900429-Gene Expression Regulation, Enzymologic, pubmed-meshheading:1900429-Glutamine, pubmed-meshheading:1900429-Ligands, pubmed-meshheading:1900429-Lysine, pubmed-meshheading:1900429-Molecular Sequence Data, pubmed-meshheading:1900429-Mutation, pubmed-meshheading:1900429-Spectrometry, Fluorescence, pubmed-meshheading:1900429-Spectrophotometry, Atomic, pubmed-meshheading:1900429-Spectrophotometry, Infrared, pubmed-meshheading:1900429-Temperature
pubmed:year
1991
pubmed:articleTitle
Structural and ligand-binding properties of a truncated form of Bacillus anthracis adenylate cyclase and of a catalytically inactive variant in which glutamine substitutes for lysine-346.
pubmed:affiliation
Unité des Antigènes Bactériens, Institut Pasteur, Paris, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't