1nbs: Difference between revisions

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New page: left|200px<br /><applet load="1nbs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nbs, resolution 3.15Å" /> '''Crystal structure of...
 
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[[Image:1nbs.gif|left|200px]]<br /><applet load="1nbs" size="450" color="white" frame="true" align="right" spinBox="true"  
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caption="1nbs, resolution 3.15&Aring;" />
caption="1nbs, resolution 3.15&Aring;" />
'''Crystal structure of the specificity domain of Ribonuclease P RNA'''<br />
'''Crystal structure of the specificity domain of Ribonuclease P RNA'''<br />


==Overview==
==Overview==
RNase P is the only endonuclease responsible for processing the 5' end of, transfer RNA by cleaving a precursor and leading to tRNA maturation. It, contains an RNA component and a protein component and has been identified, in all organisms. It was one of the first catalytic RNAs identified and, the first that acts as a multiple-turnover enzyme in vivo. RNase P and the, ribosome are so far the only two ribozymes known to be conserved in all, kingdoms of life. The RNA component of bacterial RNase P can catalyse, pre-tRNA cleavage in the absence of the RNase P protein in vitro and, consists of two domains: a specificity domain and a catalytic domain. Here, we report a 3.15-A resolution crystal structure of the 154-nucleotide, specificity domain of Bacillus subtilis RNase P. The structure reveals the, architecture of this domain, the interactions that maintain the overall, fold of the molecule, a large non-helical but well-structured module that, is conserved in all RNase P RNA, and the regions that are involved in, interactions with the substrate.
RNase P is the only endonuclease responsible for processing the 5' end of transfer RNA by cleaving a precursor and leading to tRNA maturation. It contains an RNA component and a protein component and has been identified in all organisms. It was one of the first catalytic RNAs identified and the first that acts as a multiple-turnover enzyme in vivo. RNase P and the ribosome are so far the only two ribozymes known to be conserved in all kingdoms of life. The RNA component of bacterial RNase P can catalyse pre-tRNA cleavage in the absence of the RNase P protein in vitro and consists of two domains: a specificity domain and a catalytic domain. Here we report a 3.15-A resolution crystal structure of the 154-nucleotide specificity domain of Bacillus subtilis RNase P. The structure reveals the architecture of this domain, the interactions that maintain the overall fold of the molecule, a large non-helical but well-structured module that is conserved in all RNase P RNA, and the regions that are involved in interactions with the substrate.


==About this Structure==
==About this Structure==
1NBS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with MG and PB as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NBS OCA].  
1NBS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=PB:'>PB</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NBS OCA].  


==Reference==
==Reference==
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[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Krasilnikov, A.S.]]
[[Category: Krasilnikov, A S.]]
[[Category: Mondragon, A.]]
[[Category: Mondragon, A.]]
[[Category: Pan, T.]]
[[Category: Pan, T.]]
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[[Category: s-domain]]
[[Category: s-domain]]


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Revision as of 15:04, 21 February 2008

File:1nbs.gif


1nbs, resolution 3.15Å

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Crystal structure of the specificity domain of Ribonuclease P RNA

OverviewOverview

RNase P is the only endonuclease responsible for processing the 5' end of transfer RNA by cleaving a precursor and leading to tRNA maturation. It contains an RNA component and a protein component and has been identified in all organisms. It was one of the first catalytic RNAs identified and the first that acts as a multiple-turnover enzyme in vivo. RNase P and the ribosome are so far the only two ribozymes known to be conserved in all kingdoms of life. The RNA component of bacterial RNase P can catalyse pre-tRNA cleavage in the absence of the RNase P protein in vitro and consists of two domains: a specificity domain and a catalytic domain. Here we report a 3.15-A resolution crystal structure of the 154-nucleotide specificity domain of Bacillus subtilis RNase P. The structure reveals the architecture of this domain, the interactions that maintain the overall fold of the molecule, a large non-helical but well-structured module that is conserved in all RNase P RNA, and the regions that are involved in interactions with the substrate.

About this StructureAbout this Structure

1NBS is a Single protein structure of sequence from Bacillus subtilis with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the specificity domain of ribonuclease P., Krasilnikov AS, Yang X, Pan T, Mondragon A, Nature. 2003 Feb 13;421(6924):760-4. PMID:12610630

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