Rhizobium meliloti adenylate cyclase: probing of a NTP-binding site common to cyclases and cation transporters.
Alignments between amino acid sequences of eukaryotic adenylate (ACase) and guanylate (GCase) cyclases and the prokaryotic Rhizobium meliloti ACase revealed four conserved regions. Two were the target of site-directed mutagenesis. A positive charge at position 44 converted the enzyme to GCase, a negative charge at this position had no effect. A second modification indicated that residues 107 and 124 contribute to the nucleoside triphosphate binding pocket's conformation. This latter region was used to scan protein sequences data banks. A similar region was detected in the family of E1-E2 type ATPases. Topographical resemblance between these ATPases, eukaryotic ACases and several transporters suggest that they evolved from a common ancestor.
Beuve
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A
CNRS URA 1129, Département de Biochimie et Génétique Moléculaire, Institut Pasteur, Paris, France.
Krin
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E
Danchin
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A
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000262:Adenylyl Cyclases / Q000378:metabolism*; D001665:Binding Sites; D001692:Biological Transport; D002412:Cations / Q000378:metabolism; D005057:Eukaryotic Cells / Q000201:enzymology; D006162:Guanylate Cyclase / Q000378:metabolism; D066298:In Vitro Techniques; D009711:Nucleotides / Q000378:metabolism*; D016415:Sequence Alignment; D016962:Sinorhizobium meliloti / Q000201:enzymology*; D013379:Substrate Specificity
D002412:Cations; D009711:Nucleotides; D000251:Adenosine Triphosphatases; D000262:Adenylyl Cyclases; D006162:Guanylate Cyclase