2r92

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2r92.gif|left|200px]]<br /><applet load="2r92" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:2r92.gif|left|200px]]
-
caption="2r92, resolution 3.80&Aring;" />
+
 
-
'''Elongation complex of RNA polymerase II with artificial RdRP scaffold'''<br />
+
{{Structure
 +
|PDB= 2r92 |SIZE=350|CAPTION= <scene name='initialview01'>2r92</scene>, resolution 3.80&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene>
 +
|ACTIVITY= [http://en.wikipedia.org/wiki/DNA-directed_RNA_polymerase DNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.6 2.7.7.6]
 +
|GENE=
 +
}}
 +
 
 +
'''Elongation complex of RNA polymerase II with artificial RdRP scaffold'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
2R92 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/DNA-directed_RNA_polymerase DNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.6 2.7.7.6] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R92 OCA].
+
2R92 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R92 OCA].
==Reference==
==Reference==
-
Molecular basis of RNA-dependent RNA polymerase II activity., Lehmann E, Brueckner F, Cramer P, Nature. 2007 Nov 15;450(7168):445-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18004386 18004386]
+
Molecular basis of RNA-dependent RNA polymerase II activity., Lehmann E, Brueckner F, Cramer P, Nature. 2007 Nov 15;450(7168):445-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18004386 18004386]
[[Category: DNA-directed RNA polymerase]]
[[Category: DNA-directed RNA polymerase]]
[[Category: Protein complex]]
[[Category: Protein complex]]
Line 48: Line 57:
[[Category: zinc-finger]]
[[Category: zinc-finger]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:45:32 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:33:41 2008''

Revision as of 16:33, 20 March 2008

Image:2r92.gif


PDB ID 2r92

Drag the structure with the mouse to rotate
, resolution 3.80Å
Ligands: and
Activity: DNA-directed RNA polymerase, with EC number 2.7.7.6
Coordinates: save as pdb, mmCIF, xml



Elongation complex of RNA polymerase II with artificial RdRP scaffold


Overview

RNA polymerase (Pol) II catalyses DNA-dependent RNA synthesis during gene transcription. There is, however, evidence that Pol II also possesses RNA-dependent RNA polymerase (RdRP) activity. Pol II can use a homopolymeric RNA template, can extend RNA by several nucleotides in the absence of DNA, and has been implicated in the replication of the RNA genomes of hepatitis delta virus (HDV) and plant viroids. Here we show the intrinsic RdRP activity of Pol II with only pure polymerase, an RNA template-product scaffold and nucleoside triphosphates (NTPs). Crystallography reveals the template-product duplex in the site occupied by the DNA-RNA hybrid during transcription. RdRP activity resides at the active site used during transcription, but it is slower and less processive than DNA-dependent activity. RdRP activity is also obtained with part of the HDV antigenome. The complex of transcription factor IIS (TFIIS) with Pol II can cleave one HDV strand, create a reactive stem-loop in the hybrid site, and extend the new RNA 3' end. Short RNA stem-loops with a 5' extension suffice for activity, but their growth to a critical length apparently impairs processivity. The RdRP activity of Pol II provides a missing link in molecular evolution, because it suggests that Pol II evolved from an ancient replicase that duplicated RNA genomes.

About this Structure

2R92 is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Molecular basis of RNA-dependent RNA polymerase II activity., Lehmann E, Brueckner F, Cramer P, Nature. 2007 Nov 15;450(7168):445-9. PMID:18004386

Page seeded by OCA on Thu Mar 20 18:33:41 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2r92"
Personal tools