期刊
MOLECULAR CELL
卷 9, 期 3, 页码 685-694出版社
CELL PRESS
DOI: 10.1016/S1097-2765(02)00480-X
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资金
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R37AI015650, R01AI015650, R01AI048660] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM059456] Funding Source: NIH RePORTER
- NIAID NIH HHS [R01 AI048660-04, AI48660, R01 AI048660-03, R01 AI048660-01A1, R01 AI048660-05, R01 AI048660, R01 AI048660-02, AI15650] Funding Source: Medline
- NIGMS NIH HHS [GM59456] Funding Source: Medline
Synthesis and detection of acyll-homoserine lactones (AHLs) enables many gram-negative bacteria to engage in quorum sensing, an intercellular signaling mechanism that activates differentiation to virulent and biofilm lifestyles. The AHL synthases catalyze acylation of S-adenosyl-L-methionine by acyl-acyl carrier protein and lactonization of the methionine moiety to give AHLs. The crystal structure of the AHL synthase, Esal, determined at 1.8 Angstrom resolution, reveals a remarkable structural similarity to the N-acetyltransferases and defines a common phosphopantetheine binding fold as the catalytic core. Critical residues responsible for catalysis and acyl chain specificity have been identified from a modeled substrate complex and verified through functional analysis in vivo. A mechanism for the N-acylation of S-adenosyl-L-methionine by 3-oxohexanoyl-acyl carrier protein is proposed.
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