1HQM

CRYSTAL STRUCTURE OF THERMUS AQUATICUS CORE RNA POLYMERASE-INCLUDES COMPLETE STRUCTURE WITH SIDE-CHAINS (EXCEPT FOR DISORDERED REGIONS)-FURTHER REFINED FROM ORIGINAL DEPOSITION-CONTAINS ADDITIONAL SEQUENCE INFORMATION

Replaces:  1DDQ

Summary for 1HQM

• Entry DOI: 10.2210/pdb1hqm/pdb
• Descriptor: DNA-directed RNA polymerase subunit alpha, DNA-directed RNA polymerase subunit beta, DNA-directed RNA polymerase subunit beta', ... (6 entities in total)
• Functional Keywords: transferase, dna-directed rna polymerase
• Biological source: Thermus aquaticus; More
• Total number of polymer chains: 5
• Total formula weight: 347937.78

Authors

Minakhin, L.,Bhagat, S.,Brunning, A.,Campbell, E.A.,Darst, S.A.,Ebright, R.H.,Severinov, K. (deposition date: 2000-12-18, release date: 2001-02-07, Last modification date: 2024-02-07)

Primary citation

Minakhin, L.,Bhagat, S.,Brunning, A.,Campbell, E.A.,Darst, S.A.,Ebright, R.H.,Severinov, K.
Bacterial RNA polymerase subunit omega and eukaryotic RNA polymerase subunit RPB6 are sequence, structural, and functional homologs and promote RNA polymerase assembly.
Proc.Natl.Acad.Sci.USA, 98:892-897, 2001

PubMed Abstract: Bacterial DNA-dependent RNA polymerase (RNAP) has subunit composition beta'betaalpha(I)alpha(II)omega. The role of omega has been unclear. We show that omega is homologous in sequence and structure to RPB6, an essential subunit shared in eukaryotic RNAP I, II, and III. In Escherichia coli, overproduction of omega suppresses the assembly defect caused by substitution of residue 1362 of the largest subunit of RNAP, beta'. In yeast, overproduction of RPB6 suppresses the assembly defect caused by the equivalent substitution in the largest subunit of RNAP II, RPB1. High-resolution structural analysis of the omega-beta' interface in bacterial RNAP, and comparison with the RPB6-RPB1 interface in yeast RNAP II, confirms the structural relationship and suggests a "latching" mechanism for the role of omega and RPB6 in promoting RNAP assembly.

PubMed: 11158566
DOI: 10.1073/pnas.98.3.892

Experimental method

X-RAY DIFFRACTION (3.3 Å)