4C3J

Structure of 14-subunit RNA polymerase I at 3.35 A resolution, crystal form C2-90

Summary for 4C3J

• Entry DOI: 10.2210/pdb4c3j/pdb
• Related: 4C3H 4C3I
• Descriptor: DNA-DIRECTED RNA POLYMERASE I SUBUNIT RPA190, DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC5, DNA-DIRECTED RNA POLYMERASES I AND III SUBUNIT RPAC2, ... (15 entities in total)
• Functional Keywords: transcription
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); More
• Cellular location: Nucleus, nucleolus: P10964 P22139 P28000 P40422 Q01080 P47006 P22138 P07703 P50106 P46669 P32529; Nucleus: P20434 P20436; Cytoplasm: P20435
• Total number of polymer chains: 14
• Total formula weight: 590722.37

Authors

Fernandez-Tornero, C.,Moreno-Morcillo, M.,Rashid, U.J.,Taylor, N.M.I.,Ruiz, F.M.,Gruene, T.,Legrand, P.,Steuerwald, U.,Muller, C.W. (deposition date: 2013-08-24, release date: 2013-10-23, Last modification date: 2024-05-08)

Primary citation

Fernandez-Tornero, C.,Moreno-Morcillo, M.,Rashid, U.J.,Taylor, N.M.I.,Ruiz, F.M.,Gruene, T.,Legrand, P.,Steuerwald, U.,Muller, C.W.
Crystal Structure of the 14-Subunit RNA Polymerase I
Nature, 502:644-, 2013

PubMed Abstract: Protein biosynthesis depends on the availability of ribosomes, which in turn relies on ribosomal RNA production. In eukaryotes, this process is carried out by RNA polymerase I (Pol I), a 14-subunit enzyme, the activity of which is a major determinant of cell growth. Here we present the crystal structure of Pol I from Saccharomyces cerevisiae at 3.0 Å resolution. The Pol I structure shows a compact core with a wide DNA-binding cleft and a tightly anchored stalk. An extended loop mimics the DNA backbone in the cleft and may be involved in regulating Pol I transcription. Subunit A12.2 extends from the A190 jaw to the active site and inserts a transcription elongation factor TFIIS-like zinc ribbon into the nucleotide triphosphate entry pore, providing insight into the role of A12.2 in RNA cleavage and Pol I insensitivity to α-amanitin. The A49-A34.5 heterodimer embraces subunit A135 through extended arms, thereby contacting and potentially regulating subunit A12.2.

PubMed: 24153184
DOI: 10.1038/NATURE12636

Experimental method

X-RAY DIFFRACTION (3.35 Å)