4C2M

Structure of RNA polymerase I at 2.8 A resolution

Summary for 4C2M

• Entry DOI: 10.2210/pdb4c2m/pdb
• Descriptor: DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC 4, DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC 2, DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC 3, ... (17 entities in total)
• Functional Keywords: transcription, ribosome biogenesis
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); More
• Cellular location: Nucleus, nucleolus : P40422 P32529 P22139 P28000 Q01080 P47006 P46669 P10964 P22138 P07703 P50106; Cytoplasm : P20435; Nucleus : P20436 P20434
• Total number of polymer chains: 30
• Total formula weight: 1254194.62

Authors

Engel, C.,Sainsbury, S.,Cheung, A.C.,Kostrewa, D.,Cramer, P. (deposition date: 2013-08-19, release date: 2013-10-23, Last modification date: 2024-10-23)

Primary citation

Engel, C.,Sainsbury, S.,Cheung, A.C.,Kostrewa, D.,Cramer, P.
RNA Polymerase I Structure and Transcription Regulation.
Nature, 502:502-, 2013

PubMed Abstract: Transcription of ribosomal RNA by RNA polymerase (Pol) I initiates ribosome biogenesis and regulates eukaryotic cell growth. The crystal structure of Pol I from the yeast Saccharomyces cerevisiae at 2.8 Å resolution reveals all 14 subunits of the 590-kilodalton enzyme, and shows differences to Pol II. An 'expander' element occupies the DNA template site and stabilizes an expanded active centre cleft with an unwound bridge helix. A 'connector' element invades the cleft of an adjacent polymerase and stabilizes an inactive polymerase dimer. The connector and expander must detach during Pol I activation to enable transcription initiation and cleft contraction by convergent movement of the polymerase 'core' and 'shelf' modules. Conversion between an inactive expanded and an active contracted polymerase state may generally underlie transcription. Regulatory factors can modulate the core-shelf interface that includes a 'composite' active site for RNA chain initiation, elongation, proofreading and termination.

PubMed: 24153182
DOI: 10.1038/NATURE12712

Experimental method

X-RAY DIFFRACTION (2.8 Å)