1WCM

Complete 12-Subunit RNA Polymerase II at 3.8 Angstrom

Summary for 1WCM

• Entry DOI: 10.2210/pdb1wcm/pdb
• Related: 1I3Q 1I50 1I6H 1K83 1NIK 1NT9 1PQV 1R5U 1R9S 1R9T 1SFO 1TWA 1TWC 1TWF 1TWG 1TWH
• Descriptor: DNA-DIRECTED RNA POLYMERASE II LARGEST SUBUNIT, DNA-DIRECTED RNA POLYMERASES I, II AND III 8.3 KDA POLYPEPTIDE, DNA-DIRECTED RNA POLYMERASE II 13.6 KDA POLYPEPTIDE, ... (14 entities in total)
• Functional Keywords: dna-binding, dna-directed rna polymerase, dna-dependent rna polymerase, cellular rna polymerase, multisubunit co, metal- binding, nuclear protein, transcription, phosphorylation, transferase, zinc, zinc-finger
• Biological source: SACCHAROMYCES CEREVISIAE (YEAST); More
• Cellular location: Nucleus: P04050 P08518 P16370 P20434 P20436 P27999 P38902; Nucleus, nucleolus: P40422 P22139; Cytoplasm: P20435
• Total number of polymer chains: 12
• Total formula weight: 509588.55

Authors

Armache, K.-J.,Mitterweger, S.,Meinhart, A.,Cramer, P. (deposition date: 2004-11-17, release date: 2004-12-14, Last modification date: 2024-10-09)

Primary citation

Armache, K.-J.,Mitterweger, S.,Meinhart, A.,Cramer, P.
Structures of Complete RNA Polymerase II and its Subcomplex,Rpb4/7
J.Biol.Chem., 280:7131-, 2005

PubMed Abstract: We determined the x-ray structure of the RNA polymerase (Pol) II subcomplex Rpb4/7 at 2.3 A resolution, combined it with a previous structure of the 10-subunit polymerase core, and refined an atomic model of the complete 12-subunit Pol II at 3.8-A resolution. Comparison of the complete Pol II structure with structures of the Pol II core and free Rpb4/7 shows that the core-Rpb4/7 interaction goes along with formation of an alpha-helix in the linker region of the largest Pol II subunit and with folding of the conserved Rpb7 tip loop. Details of the core-Rpb4/7 interface explain facilitated Rpb4/7 dissociation in a temperature-sensitive Pol II mutant and specific assembly of Pol I with its Rpb4/7 counterpart, A43/14. The refined atomic model of Pol II serves as the new reference structure for analysis of the transcription mechanism and enables structure solution of complexes of the complete enzyme with additional factors and nucleic acids by molecular replacement.

PubMed: 15591044
DOI: 10.1074/JBC.M413038200

Experimental method

X-RAY DIFFRACTION (3.8 Å)