PMID:16181146 - Revision history

imported>Wikientrybot: change PMID template to TableEdit version

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	'''~~No author listed~~''' (2005) The molecular basis for the mode of action of bicyclomycin. ''Curr Drug Targets Infect Disord'' '''5''':273-95		'''Kohn, H and Widger, W''' (2005) The molecular basis for the mode of action of bicyclomycin. ''Curr Drug Targets Infect Disord'' '''5''':273-95
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 ==EcoliWiki Links {{HelpIcon|Help:Literature}} ==

imported>Wikientrybot: change PMID template to TableEdit version

2013-09-01T18:48:54Z

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← Older revision		Revision as of 18:48, 1 September 2013
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	<~~protect~~>		<!--box uid=d41d8cd98f00b204e9800998ecf8427e.180715.Y52238c1653b53-->
	<~~span style = 'font~~-~~size: large'> '''Kohn, H and Widger, W''~~' ~~(2005) The molecular basis for~~ the ~~mode of action of bicyclomycin~~.~~''Curr Drug Targets Infect Disord'' '''5''':273~~-~~95</span~~>		<!--
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	\|~~{{TableHeadingColor}}~~ \|'''~~Abstract~~''' \|\| <protect>Bicyclomycin (1) is a clinically useful antibiotic exhibiting activity against a broad spectrum of Gram-negative bacteria and against the Gram-positive bacterium, Micrococcus luteus. Bicyclomycin has been used to treat diarrhea in humans and bacterial diarrhea in calves and pigs and is marketed by Fujisawa (~~Osaka, Japan~~) ~~under the trade name Bicozamycin.~~ The structure of 1 is unique among antibiotics, and our studies document that its mechanism of action is novel. Early mechanistic proposals suggested that 1 reacted with nucleophiles (e.g., a protein sulfhydryl group) necessary for the remodeling the peptidoglycan assembly within the bacterial cell wall. We, however, showed that 1 targeted the rho transcription termination factor in Escherichia coli. The rho protein is integral to the expression of ~~many gene products in E. coli and other Gram-negative bacteria, and without rho the cell losses viability. Rho is a member~~ of ~~the RecA-type ATPase class of enzymes that use nucleotide contacts to couple oligonucleotide translocation to ATP hydrolysis~~. ~~Bicyclomycin is the only known selective inhibitor of rho. In this article, we integrate the evidence obtained from bicyclomycin structure~~-activity studies, site-directed mutagenesis investigations, bicyclomycin affinity labels, and biochemical and biophysical measurements with recent X-ray crystallographic images of the bicyclomycin-rho complex to define the rho antibiotic binding site and to document the pathway for rho inhibition by 1. Together, the structural and functional studies demonstrate how 1, a modest rho inhibitor, can disrupt the rho molecular machinery thereby leading to a catastrophic effect caused by the untimely overproduction of proteins not normally expressed constitutively, thus leading to a toxic effect on the cells.</protect>		!align=left \|Citation
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			'''No author listed''' (2005) The molecular basis for the mode of action of bicyclomycin. ''Curr Drug Targets Infect Disord'' '''5''':273-95
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	\|~~{{TableHeadingColor}} nowrap~~ \|~~'''~~Links~~'''~~ \|\|		!align=left \|Abstract
	* [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=16181146 PubMed]		\|\|
			Bicyclomycin (1) is a clinically useful antibiotic exhibiting activity against a broad spectrum of Gram-negative bacteria and against the Gram-positive bacterium, Micrococcus luteus. Bicyclomycin has been used to treat diarrhea in humans and bacterial diarrhea in calves and pigs and is marketed by Fujisawa (Osaka, Japan) under the trade name Bicozamycin. The structure of 1 is unique among antibiotics, and our studies document that its mechanism of action is novel. Early mechanistic proposals suggested that 1 reacted with nucleophiles (e.g., a protein sulfhydryl group) necessary for the remodeling the peptidoglycan assembly within the bacterial cell wall. We, however, showed that 1 targeted the rho transcription termination factor in Escherichia coli. The rho protein is integral to the expression of many gene products in E. coli and other Gram-negative bacteria, and without rho the cell losses viability. Rho is a member of the RecA-type ATPase class of enzymes that use nucleotide contacts to couple oligonucleotide translocation to ATP hydrolysis. Bicyclomycin is the only known selective inhibitor of rho. In this article, we integrate the evidence obtained from bicyclomycin structure-activity studies, site-directed mutagenesis investigations, bicyclomycin affinity labels, and biochemical and biophysical measurements with recent X-ray crystallographic images of the bicyclomycin-rho complex to define the rho antibiotic binding site and to document the pathway for rho inhibition by 1. Together, the structural and functional studies demonstrate how 1, a modest rho inhibitor, can disrupt the rho molecular machinery thereby leading to a catastrophic effect caused by the untimely overproduction of proteins not normally expressed constitutively, thus leading to a toxic effect on the cells.
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			[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=16181146 PubMed]

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			!align=left \|Keywords
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			Adenosine Triphosphatases/antagonists & inhibitors; Adenosine Triphosphatases/chemistry; Anti-Bacterial Agents/chemistry; Anti-Bacterial Agents/metabolism; Anti-Bacterial Agents/pharmacology; Bicyclo Compounds, Heterocyclic/chemistry; Bicyclo Compounds, Heterocyclic/metabolism; Bicyclo Compounds, Heterocyclic/pharmacology; Binding Sites; Enzyme Inhibitors/pharmacology; Escherichia coli/enzymology; Humans; Models, Chemical; Models, Molecular; Molecular Structure; Mutation; Protein Binding; Protein Conformation; Protein Structure, Tertiary; RNA, Bacterial/metabolism; Rho Factor/antagonists & inhibitors; Rho Factor/chemistry; Rho Factor/genetics; Structure-Activity Relationship; Transcription, Genetic/drug effects

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	==Significance {{HelpIcon\|Help:Literature}} ==		==Significance {{HelpIcon\|Help:Literature}} ==
	{{LitSignificance}}		{{LitSignificance}}

165.91.108.111: Fill PMID: Page!

2011-10-18T15:22:34Z

Fill PMID: Page!

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		<protect>
		<span style = 'font-size: large'> '''Kohn, H and Widger, W''' (2005) The molecular basis for the mode of action of bicyclomycin.''Curr Drug Targets Infect Disord'' '''5''':273-95</span>

		{\|{{Prettytable}} align = 'center' width= '70%'
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		\|{{TableHeadingColor}} \|'''Abstract''' \|\| <protect>Bicyclomycin (1) is a clinically useful antibiotic exhibiting activity against a broad spectrum of Gram-negative bacteria and against the Gram-positive bacterium, Micrococcus luteus. Bicyclomycin has been used to treat diarrhea in humans and bacterial diarrhea in calves and pigs and is marketed by Fujisawa (Osaka, Japan) under the trade name Bicozamycin. The structure of 1 is unique among antibiotics, and our studies document that its mechanism of action is novel. Early mechanistic proposals suggested that 1 reacted with nucleophiles (e.g., a protein sulfhydryl group) necessary for the remodeling the peptidoglycan assembly within the bacterial cell wall. We, however, showed that 1 targeted the rho transcription termination factor in Escherichia coli. The rho protein is integral to the expression of many gene products in E. coli and other Gram-negative bacteria, and without rho the cell losses viability. Rho is a member of the RecA-type ATPase class of enzymes that use nucleotide contacts to couple oligonucleotide translocation to ATP hydrolysis. Bicyclomycin is the only known selective inhibitor of rho. In this article, we integrate the evidence obtained from bicyclomycin structure-activity studies, site-directed mutagenesis investigations, bicyclomycin affinity labels, and biochemical and biophysical measurements with recent X-ray crystallographic images of the bicyclomycin-rho complex to define the rho antibiotic binding site and to document the pathway for rho inhibition by 1. Together, the structural and functional studies demonstrate how 1, a modest rho inhibitor, can disrupt the rho molecular machinery thereby leading to a catastrophic effect caused by the untimely overproduction of proteins not normally expressed constitutively, thus leading to a toxic effect on the cells.</protect>
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		* [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=16181146 PubMed]

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		==Significance {{HelpIcon\|Help:Literature}} ==
		{{LitSignificance}}

		== Useful Materials and Methods {{HelpIcon\|Help:Literature}}==
		{{LitMaterials}}

		==Annotations {{HelpIcon\|Help:Literature}}==
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		!\|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status

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		==See also==

		==References==
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		<references/>

165.91.108.111: New PMID: Page!

2011-10-18T15:22:34Z

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