Functional sites and evolutionary connections of acylhomoserine lactone synthases

Chakrabarti, Saikat ; Sowdhamini, R. (2003) Functional sites and evolutionary connections of acylhomoserine lactone synthases Protein Engineering Design and Selection, 16 (4). pp. 271-278. ISSN 1741-0126

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Official URL: http://peds.oxfordjournals.org/content/16/4/271.ab...

Related URL: http://dx.doi.org/10.1093/proeng/gzg031

Abstract

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.

Item Type:Article
Source:Copyright of this article belongs to Oxford University Press.
Keywords:Distant Similarity; Intermediate Sequences; N-acetyl Transferase; OHHL Synthase; Protein Structure Prediction; Quorum Sensing
ID Code:61267
Deposited On:15 Sep 2011 03:55
Last Modified:15 Sep 2011 03:55

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