1dzf
From Proteopedia
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(New page: 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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Revision as of 11:34, 20 November 2007
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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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