4YG2

X-ray crystal structur of Escherichia coli RNA polymerase sigma70 holoenzyme

Replaces:  4IGC

Summary for 4YG2

• Entry DOI: 10.2210/pdb4yg2/pdb
• Related: 4IGC 4YFK 4YFN 4YFX
• Descriptor: DNA-directed RNA polymerase subunit alpha, DNA-directed RNA polymerase subunit beta, DNA-directed RNA polymerase subunit beta', ... (7 entities in total)
• Functional Keywords: rna polymerase, transferase-transcription complex, transferase/transcription
• Biological source: Escherichia coli O157:H7; More
• Total number of polymer chains: 12
• Total formula weight: 920172.47

Authors

Murakami, K.S. (deposition date: 2015-02-25, release date: 2015-03-18, Last modification date: 2024-02-28)

Primary citation

Murakami, K.S.
X-ray crystal structure of Escherichia coli RNA polymerase sigma70 holoenzyme
J. Biol. Chem., 288:9126-9134, 2013

PubMed Abstract: Escherichia coli RNA polymerase (RNAP) is the most studied bacterial RNAP and has been used as the model RNAP for screening and evaluating potential RNAP-targeting antibiotics. However, the x-ray crystal structure of E. coli RNAP has been limited to individual domains. Here, I report the x-ray structure of the E. coli RNAP σ(70) holoenzyme, which shows σ region 1.1 (σ1.1) and the α subunit C-terminal domain for the first time in the context of an intact RNAP. σ1.1 is positioned at the RNAP DNA-binding channel and completely blocks DNA entry to the RNAP active site. The structure reveals that σ1.1 contains a basic patch on its surface, which may play an important role in DNA interaction to facilitate open promoter complex formation. The α subunit C-terminal domain is positioned next to σ domain 4 with a fully stretched linker between the N- and C-terminal domains. E. coli RNAP crystals can be prepared from a convenient overexpression system, allowing further structural studies of bacterial RNAP mutants, including functionally deficient and antibiotic-resistant RNAPs.

PubMed: 23389035
DOI: 10.1074/jbc.M112.430900

Experimental method

X-RAY DIFFRACTION (3.7 Å)