1nbs: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 1: Line 1:
[[Image:1nbs.gif|left|200px]]<br /><applet load="1nbs" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1nbs.gif|left|200px]]
caption="1nbs, resolution 3.15&Aring;" />
 
'''Crystal structure of the specificity domain of Ribonuclease P RNA'''<br />
{{Structure
|PDB= 1nbs |SIZE=350|CAPTION= <scene name='initialview01'>1nbs</scene>, resolution 3.15&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=PB:LEAD (II) ION'>PB</scene>
|ACTIVITY=
|GENE=
}}
 
'''Crystal structure of the specificity domain of Ribonuclease P RNA'''
 


==Overview==
==Overview==
Line 7: Line 16:


==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 <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].  
1NBS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NBS OCA].  


==Reference==
==Reference==
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12610630 12610630]
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:[http://www.ncbi.nlm.nih.gov/pubmed/12610630 12610630]
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 23: Line 32:
[[Category: s-domain]]
[[Category: s-domain]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:04:23 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:54:46 2008''

Revision as of 13:54, 20 March 2008

File:1nbs.gif


PDB ID 1nbs

Drag the structure with the mouse to rotate
, resolution 3.15Å
Ligands: and
Coordinates: save as pdb, mmCIF, xml



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. 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

Page seeded by OCA on Thu Mar 20 12:54:46 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA