1DZF

RPB5 from S.cerevisiae

Summary for 1DZF

• Entry DOI: 10.2210/pdb1dzf/pdb
• Descriptor: DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC 1 (2 entities in total)
• Functional Keywords: rna polymerase, rna polymerase subunit, transferase
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• Cellular location: Nucleus: P20434
• Total number of polymer chains: 1
• Total formula weight: 25117.09

Authors

Todone, F.,Weinzierl, R.O.J.,Brick, P.,Onesti, S. (deposition date: 2000-02-25, release date: 2000-06-09, Last modification date: 2024-05-08)

Primary citation

Todone, F.,Weinzierl, R.O.J.,Brick, P.,Onesti, S.
Crystal Structure of Rpb5, a Universal Eukaryotic RNA Polymerase Subunit and Transcription Factor Interaction Target
Proc.Natl.Acad.Sci.USA, 97:6306-, 2000

PubMed Abstract: 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.

PubMed: 10841537
DOI: 10.1073/PNAS.97.12.6306

Experimental method

X-RAY DIFFRACTION (1.9 Å)