Crystal structure of the RNA-binding domain from transcription termination factor rho

1998 ◽  
Vol 5 (5) ◽  
pp. 352-356 ◽  
Author(s):  
Timothy J. Allison ◽  
Todd C. Wood ◽  
Deborah M. Briercheck ◽  
Fraydoon Rastinejad ◽  
John P. Richardson ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Rna Binding ◽  
Transcription Termination ◽  
Binding Domain ◽  
Termination Factor ◽  
Transcription Termination Factor ◽  
Rna Binding Domain

Crystal structure of the unique RNA-binding domain of the influenza virus NS1 protein

1997 ◽  
Vol 4 (11) ◽  
pp. 896-899 ◽  
Author(s):  
Jinsong Liu ◽  
Patricia A. Lynch ◽  
Chen-ya Chien ◽  
Gaetano T. Montelione ◽  
Robert M. Krug ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Influenza Virus ◽  
Rna Binding ◽  
Binding Domain ◽  
Ns1 Protein ◽  
Rna Binding Domain

scholarly journals Effects of Bicyclomycin on RNA- and ATP-Binding Activities of Transcription Termination Factor Rho

1998 ◽  
Vol 42 (3) ◽  
pp. 571-578 ◽  
Author(s):  
Lucia Carrano ◽  
Cecilia Bucci ◽  
Roberto De Pascalis ◽  
Alfredo Lavitola ◽  
Filomena Manna ◽  
...  
Keyword(s):  
Rna Binding ◽  
Transcription Termination ◽  
Gel Filtration ◽  
Experimental System ◽  
Cross Linking ◽  
Atp Binding ◽  
Mobility Shift ◽  
Termination Factor ◽  
Transcription Termination Factor

ABSTRACT Bicyclomycin is a commercially important antibiotic that has been shown to be effective against many gram-negative bacteria. Genetic and biochemical evidence indicates that the antibiotic interferes with RNA metabolism in Escherichia coli by inhibiting the activity of transcription termination factor Rho. However, the precise mechanism of inhibition is not completely known. In this study we have used in vitro transcription assays to analyze the effects of bicyclomycin on the termination step of transcription. The Rho-dependent transcription termination region located within thehisG cistron of Salmonella typhimurium has been used as an experimental system. The possible interference of the antibiotic with the various functions of factor Rho, such as RNA binding at the primary site, ATP binding, and hexamer formation, has been investigated by RNA gel mobility shift, photochemical cross-linking, and gel filtration experiments. The results of these studies demonstrate that bicyclomycin does not interfere with the binding of Rho to the loading site on nascent RNA. Binding of the factor to ATP is not impeded, on the contrary, the antibiotic appears to decrease the apparent equilibrium dissociation constant for ATP in photochemical cross-linking experiments. The available evidence suggests that this decrease might be due to an interference with the correct positioning of ATP within the nucleotide-binding pocket leading b an inherent block of ATP hydrolysis. Possibly, as a consequence of this interference, the antibiotic also prevents ATP-dependent stabilization of Rho hexamers.

Crystal structure of the RNA-binding domain of the U1 small nuclear ribonucleoprotein A

Nature ◽  
1990 ◽  
Vol 348 (6301) ◽  
pp. 515-520 ◽  
Author(s):  
Kiyoshi Nagai ◽  
Chris Oubridge ◽  
Timm H. Jessen ◽  
Jade Li ◽  
Philip R. Evans
Keyword(s):  
Crystal Structure ◽  
Rna Binding ◽  
Binding Domain ◽  
Small Nuclear Ribonucleoprotein ◽  
Rna Binding Domain ◽  
Nuclear Ribonucleoprotein

scholarly journals Crystal structure of SARS-CoV-2 nucleocapsid protein RNA binding domain reveals potential unique drug targeting sites

2020 ◽  
Author(s):  
Sisi Kang ◽  
Mei Yang ◽  
Zhongsi Hong ◽  
Liping Zhang ◽  
Zhaoxia Huang ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Nucleocapsid Protein ◽  
Rna Binding ◽  
Structural Information ◽  
Antiviral Drug ◽  
Binding Domain ◽  
Binding Studies ◽  
Terminal Domain ◽  
Rna Binding Domain

AbstractThe outbreak of coronavirus disease (COVID-19) in China caused by SARS-CoV-2 virus continually lead to worldwide human infections and deaths. It is currently no specific viral protein targeted therapeutics yet. Viral nucleocapsid protein is a potential antiviral drug target, serving multiple critical functions during the viral life cycle. However, the structural information of SARS-CoV-2 nucleocapsid protein is yet to be clear. Herein, we have determined the 2.7 Å crystal structure of the N-terminal RNA binding domain of SARS-CoV-2 nucleocapsid protein. Although overall structure is similar with other reported coronavirus nucleocapsid protein N-terminal domain, the surface electrostatic potential characteristics between them are distinct. Further comparison with mild virus type HCoV-OC43 equivalent domain demonstrates a unique potential RNA binding pocket alongside the β-sheet core. Complemented by in vitro binding studies, our data provide several atomic resolution features of SARS-CoV-2 nucleocapsid protein N-terminal domain, guiding the design of novel antiviral agents specific targeting to SARS-CoV-2.

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