4LK0

Crystal Structure Analysis of the E.coli holoenzyme/T7 Gp2 complex

Summary for 4LK0

• Entry DOI: 10.2210/pdb4lk0/pdb
• Descriptor: DNA-directed RNA polymerase subunit alpha, DNA-directed RNA polymerase subunit beta, DNA-directed RNA polymerase subunit beta', ... (8 entities in total)
• Functional Keywords: dna directed rna polymerase, transferase
• Biological source: Escherichia coli; More
• Cellular location: Cytoplasm (Potential): P00579
• Total number of polymer chains: 14
• Total formula weight: 874013.63

Authors

Bae, B.,Darst, S.A. (deposition date: 2013-07-05, release date: 2013-11-13, Last modification date: 2024-02-28)

Primary citation

Bae, B.,Davis, E.,Brown, D.,Campbell, E.A.,Wigneshweraraj, S.,Darst, S.A.
Phage T7 Gp2 inhibition of Escherichia coli RNA polymerase involves misappropriation of sigma 70 domain 1.1.
Proc.Natl.Acad.Sci.USA, 110:19772-19777, 2013

PubMed Abstract: Bacteriophage T7 encodes an essential inhibitor of the Escherichia coli host RNA polymerase (RNAP), the product of gene 2 (Gp2). We determined a series of X-ray crystal structures of E. coli RNAP holoenzyme with or without Gp2. The results define the structure and location of the RNAP σ(70) subunit domain 1.1(σ(1.1)(70)) inside the RNAP active site channel, where it must be displaced by the DNA upon formation of the open promoter complex. The structures and associated data, combined with previous results, allow for a complete delineation of the mechanism for Gp2 inhibition of E. coli RNAP. In the primary inhibition mechanism, Gp2 forms a protein-protein interaction with σ(1.1)(70), preventing the normal egress of σ(1.1)(70) from the RNAP active site channel. Gp2 thus misappropriates a domain of the RNAP holoenzyme, σ(1.1)(70), to inhibit the function of the enzyme.

PubMed: 24218560
DOI: 10.1073/pnas.1314576110

Experimental method

X-RAY DIFFRACTION (3.9103 Å)