2001
DOI: 10.1006/jmbi.2001.5027
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The 1.2 Å structure of a novel quorum-sensing protein, Bacillus subtilis LuxS 1 1Edited by J. Thornton

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Cited by 74 publications
(100 citation statements)
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“…For example, the chemotaxis and motility genes were down regulated in B. atrophaeus (see also the supplementary Table S1) The similarity between B. atrophaeus UCMB-5137 and B. amyloliquefaciens FZB42 was in activation of the genes ymcA and luxS controlling biofilm formation (Nicolas et al, 2012). It is known that luxS is also an activator of synthesis of the quorum sensing autoinducer AI-2 (Ruzheinikov et al, 2001). Activation of ylbF, which is an antagonist of the biofilm repressor SinR (Kearns et al, 2005), was also observed in B. atrophaeus UCMB-5137 treated by the root exudates.…”
Section: Comparison Of the Gene Expression Profiles Of B Atrophaeus mentioning
confidence: 99%
“…For example, the chemotaxis and motility genes were down regulated in B. atrophaeus (see also the supplementary Table S1) The similarity between B. atrophaeus UCMB-5137 and B. amyloliquefaciens FZB42 was in activation of the genes ymcA and luxS controlling biofilm formation (Nicolas et al, 2012). It is known that luxS is also an activator of synthesis of the quorum sensing autoinducer AI-2 (Ruzheinikov et al, 2001). Activation of ylbF, which is an antagonist of the biofilm repressor SinR (Kearns et al, 2005), was also observed in B. atrophaeus UCMB-5137 treated by the root exudates.…”
Section: Comparison Of the Gene Expression Profiles Of B Atrophaeus mentioning
confidence: 99%
“…The monomer has approximate dimensions 25 Å x 35 Å x 45 Å (Ruzheinikov et al 2001). Each monomer is mainly composed of a four-stranded antiparallel β-sheet and three α-helices (Ruzheinikov et al 2001).…”
Section: Introductionmentioning
confidence: 99%
“…The monomer has approximate dimensions 25 Å x 35 Å x 45 Å (Ruzheinikov et al 2001). Each monomer is mainly composed of a four-stranded antiparallel β-sheet and three α-helices (Ruzheinikov et al 2001). In the unique dimer structure, the β-sheets face each other at the dimer interface to form a β-barrel, which is flanked by the α-helices (Ruzheinikov et al 2001 (Miller and Duerre 1968).…”
Section: Introductionmentioning
confidence: 99%
See 1 more Smart Citation
“…[46][47][48] All LuxS proteins are homodimers. Each subunit is a single polypeptide chain which share a novel α-β fold consisting of four-stranded antiparallel β-sheet bordered by 3 α helices on one side and a short 3 10 helix on the other side.…”
Section: S-ribosylhomocysteinase (Luxs)mentioning
confidence: 99%