2WNM

Solution structure of Gp2

Summary for 2WNM

• Entry DOI: 10.2210/pdb2wnm/pdb
• Descriptor: GENE 2 (1 entity in total)
• Functional Keywords: small protein inhibntor bacterial rna polymerase, hydrolase
• Biological source: ENTEROBACTERIA PHAGE T7
• Total number of polymer chains: 1
• Total formula weight: 7180.98

Authors

Camara, B.,Liu, M.,Shadrinc, A.,Liu, B.,Simpson, P.,Weinzierl, R.,Severinovc, K.,Cota, E.,Matthews, S.,Wigneshweraraj, S.R. (deposition date: 2009-07-13, release date: 2010-02-16, Last modification date: 2024-05-15)

Primary citation

Camara, B.,Liu, M.,Reynolds, J.,Shadrin, A.,Liu, B.,Kwok, K.,Simpson, P.,Weinzierl, R.,Severinov, K.,Cota, E.,Matthews, S.,Wigneshweraraj, S.R.
T7 Phage Protein Gp2 Inhibits the Escherichia Coli RNA Polymerase by Antagonizing Stable DNA Strand Separation Near the Transcription Start Site.
Proc.Natl.Acad.Sci.USA, 107:2247-, 2010

PubMed Abstract: Infection of Escherichia coli by the T7 phage leads to rapid and selective inhibition of the host RNA polymerase (RNAP)--a multi-subunit enzyme responsible for gene transcription--by a small ( approximately 7 kDa) phage-encoded protein called Gp2. Gp2 is also a potent inhibitor of E. coli RNAP in vitro. Here we describe the first atomic resolution structure of Gp2, which reveals a distinct run of surface-exposed negatively charged amino acid residues on one side of the molecule. Our comprehensive mutagenesis data reveal that two conserved arginine residues located on the opposite side of Gp2 are important for binding to and inhibition of RNAP. Based on a structural model of the Gp2-RNAP complex, we propose that inhibition of transcription by Gp2 involves prevention of RNAP-promoter DNA interactions required for stable DNA strand separation and maintenance of the "transcription bubble" near the transcription start site, an obligatory step in the formation of a transcriptionally competent promoter complex.

PubMed: 20133868
DOI: 10.1073/PNAS.0907908107

Experimental method

SOLUTION NMR