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New page: left|200px<br /><applet load="1dzf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dzf, resolution 1.9Å" /> '''RPB5 FROM S.CEREVISIA...
 
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[[Image:1dzf.jpg|left|200px]]<br /><applet load="1dzf" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1dzf.jpg|left|200px]]<br /><applet load="1dzf" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1dzf, resolution 1.9&Aring;" />
caption="1dzf, resolution 1.9&Aring;" />
'''RPB5 FROM S.CEREVISIAE'''<br />
'''RPB5 FROM S.CEREVISIAE'''<br />


==Overview==
==Overview==
Eukaryotic nuclei contain three different types of RNA polymerases, (RNAPs), each consisting of 12-18 different subunits. The evolutionarily, highly conserved RNAP subunit RPB5 is shared by all three enzymes and, therefore represents a key structural/functional component of all, eukaryotic RNAPs. Here we present the crystal structure of the RPB5, subunit from Saccharomyces cerevisiae. The bipartite structure includes a, eukaryote-specific N-terminal domain and a C-terminal domain resembling, the archaeal RNAP subunit H. RPB5 has been implicated in direct, protein-protein contacts with transcription factor IIB, one of the, components of the RNAP(II) basal transcriptional machinery, and, gene-specific activator proteins, such as the hepatitis B virus, transactivator protein X. The experimentally mapped regions of RPB5, involved in these interactions correspond to distinct and surface-exposed, alpha-helical structures.
Eukaryotic nuclei contain three different types of RNA polymerases (RNAPs), each consisting of 12-18 different subunits. The evolutionarily highly conserved RNAP subunit RPB5 is shared by all three enzymes and therefore represents a key structural/functional component of all eukaryotic RNAPs. Here we present the crystal structure of the RPB5 subunit from Saccharomyces cerevisiae. The bipartite structure includes a eukaryote-specific N-terminal domain and a C-terminal domain resembling the archaeal RNAP subunit H. RPB5 has been implicated in direct protein-protein contacts with transcription factor IIB, one of the components of the RNAP(II) basal transcriptional machinery, and gene-specific activator proteins, such as the hepatitis B virus transactivator protein X. The experimentally mapped regions of RPB5 involved in these interactions correspond to distinct and surface-exposed alpha-helical structures.


==About this Structure==
==About this Structure==
1DZF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DZF OCA].  
1DZF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. 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=1DZF OCA].  


==Reference==
==Reference==
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[[Category: Onesti, S.]]
[[Category: Onesti, S.]]
[[Category: Todone, F.]]
[[Category: Todone, F.]]
[[Category: Weinzierl, R.O.J.]]
[[Category: Weinzierl, R O.J.]]
[[Category: rna polymerase subunit]]
[[Category: rna polymerase subunit]]


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Revision as of 10:22, 21 February 2008

File:1dzf.jpg


1dzf, resolution 1.9Å

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RPB5 FROM S.CEREVISIAE

Overview

Eukaryotic nuclei contain three different types of RNA polymerases (RNAPs), each consisting of 12-18 different subunits. The evolutionarily highly conserved RNAP subunit RPB5 is shared by all three enzymes and therefore represents a key structural/functional component of all eukaryotic RNAPs. Here we present the crystal structure of the RPB5 subunit from Saccharomyces cerevisiae. The bipartite structure includes a eukaryote-specific N-terminal domain and a C-terminal domain resembling the archaeal RNAP subunit H. RPB5 has been implicated in direct protein-protein contacts with transcription factor IIB, one of the components of the RNAP(II) basal transcriptional machinery, and gene-specific activator proteins, such as the hepatitis B virus transactivator protein X. The experimentally mapped regions of RPB5 involved in these interactions correspond to distinct and surface-exposed alpha-helical structures.

About this Structure

1DZF is a Single protein structure of sequence from Saccharomyces cerevisiae. Active as DNA-directed RNA polymerase, with EC number 2.7.7.6 Full crystallographic information is available from OCA.

Reference

Crystal structure of RPB5, a universal eukaryotic RNA polymerase subunit and transcription factor interaction target., Todone F, Weinzierl RO, Brick P, Onesti S, Proc Natl Acad Sci U S A. 2000 Jun 6;97(12):6306-10. PMID:10841537

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