Functional sites and evolutionary connections of acylhomoserine lactone synthases.
Acylhomoserine lactone (AHL) synthases act as chemical communication signals or pheromones in Gram-negative bacteria and regulate diverse physiological events in a cell density-dependent manner. The recent crystal structure determination of EsaI, a key enzyme in this pathway, shows that the AHL synthase superfamily members adopt the fold of the N-acetyltransferase superfamily. We suggest, by the identification of intermediate sequences, that the two superfamilies are evolutionarily related. Evolutionary trace analyses of aligned sequences and docking studies have been used to discuss functionally important residues of EsaI homologues.
National Centre for Biological Sciences, Tata Institute of Fundamental Research, UAS-GKVK Campus, Bangalore 560 065, India.
Saikat
S
Chakrabarti
R
R
Sowdhamini
D000123:Acetyltransferases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D000595:Amino Acid Sequence; D001665:Binding Sites; D002265:Carboxylic Ester Hydrolases / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D018360:Crystallography, X-Ray; D006090:Gram-Negative Bacteria / Q000378:metabolism; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D008968:Molecular Conformation; D008969:Molecular Sequence Data; D010204:Pantetheine / Q000031:analogs & derivatives* / Q000737:chemistry; D016415:Sequence Alignment; D013379:Substrate Specificity
D010204:Pantetheine; D000123:Acetyltransferases; D002265:Carboxylic Ester Hydrolases; C432003:N-acyl homoserine lactonase; C003129:4'-phosphopantetheine