4LLG: Crystal Structure Analysis Of The E.coli Holoenzyme/gp2 Complex

Citation:
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 sigma(70) subunit domain 1.1 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 , preventing the normal egress of from the RNAP active site channel. Gp2 thus misappropriates a domain of the RNAP holoenzyme, , to inhibit the function of the enzyme.
PDB ID: 4LLGDownload
MMDB ID: 115118
PDB Deposition Date: 2013/7/9
Updated in MMDB: 2013/12
Experimental Method:
x-ray diffraction
Resolution: 3.79  Å
Source Organism:
Escherichia coli BW2952
Similar Structures:
Biological Unit for 4LLG: heptameric; determined by author and by software (PISA)
Molecular Components in 4LLG
Label Count Molecule
Proteins (7 molecules)
2
DNA-directed RNA Polymerase Subunit Alpha
Molecule annotation
1
DNA-directed RNA Polymerase Subunit Beta
Molecule annotation
1
DNA-directed RNA Polymerase Subunit Beta'
Molecule annotation
1
DNA-directed RNA Polymerase Subunit Omega
Molecule annotation
1
RNA Polymerase Sigma Factor Rpod(Gene symbol: rpoD)
Molecule annotation
1
Bacterial RNA Polymerase Inhibitor(Gene symbol: T7p16)
Molecule annotation
Chemicals (3 molecules)
1
1
2
2
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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