Structural basis of acyl-homoserine lactone-dependent signaling.
Department of Pharmacology and Program in Structural Biology and Biophysics, The University of Colorado School of Medicine, Aurora, Colorado 80045, USA. mair.churchill@ucdenver.edu
Mair E A
ME
Churchill
Lingling
L
Chen
D054742:Acyl-Butyrolactones / Q000737:chemistry* / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D004247:DNA / Q000737:chemistry / Q000378:metabolism; D008025:Ligases / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D012097:Repressor Proteins / Q000737:chemistry / Q000378:metabolism; D015398:Signal Transduction; D015534:Trans-Activators / Q000737:chemistry / Q000378:metabolism
D054742:Acyl-Butyrolactones; D001426:Bacterial Proteins; D012097:Repressor Proteins; D015534:Trans-Activators; C074281:TraM protein, bacterial; C064778:LuxR autoinducer binding proteins; D004247:DNA; D008025:Ligases; C449816:N-acylhomoserine lactone synthase