5EZK

RNA polymerase model placed by Molecular replacement into X-ray diffraction map of DNA-bound RNA Polymerase-Sigma 54 holoenzyme complex.

Summary for 5EZK

• Entry DOI: 10.2210/pdb5ezk/pdb
• Descriptor: DNA-directed RNA polymerase subunit alpha, DNA-directed RNA polymerase subunit beta, DNA-directed RNA polymerase subunit beta', ... (4 entities in total)
• Functional Keywords: rna polymerase, transferase
• Biological source: Escherichia coli; More
• Total number of polymer chains: 5
• Total formula weight: 389554.56

Authors

Darbari, V.C.,Yang, Y.,Lu, D.,Zhang, N.,Glyde, R.,Wang, Y.,Murakami, K.S.,Buck, M.,Zhang, X. (deposition date: 2015-11-26, release date: 2015-12-16, Last modification date: 2024-01-10)

Primary citation

Yang, Y.,Darbari, V.C.,Zhang, N.,Lu, D.,Glyde, R.,Wang, Y.P.,Winkelman, J.T.,Gourse, R.L.,Murakami, K.S.,Buck, M.,Zhang, X.
TRANSCRIPTION. Structures of the RNA polymerase- Sigma 54 reveal new and conserved regulatory strategies.
Science, 349:882-885, 2015

PubMed Abstract: Transcription by RNA polymerase (RNAP) in bacteria requires specific promoter recognition by σ factors. The major variant σ factor (σ(54)) initially forms a transcriptionally silent complex requiring specialized adenosine triphosphate-dependent activators for initiation. Our crystal structure of the 450-kilodalton RNAP-σ(54) holoenzyme at 3.8 angstroms reveals molecular details of σ(54) and its interactions with RNAP. The structure explains how σ(54) targets different regions in RNAP to exert its inhibitory function. Although σ(54) and the major σ factor, σ(70), have similar functional domains and contact similar regions of RNAP, unanticipated differences are observed in their domain arrangement and interactions with RNAP, explaining their distinct properties. Furthermore, we observe evolutionarily conserved regulatory hotspots in RNAPs that can be targeted by a diverse range of mechanisms to fine tune transcription.

PubMed: 26293966
DOI: 10.1126/science.aab1478

Experimental method

X-RAY DIFFRACTION (8.5 Å)