2lmc
From Proteopedia
Structure of T7 transcription factor Gp2-E. coli RNAp jaw domain complex
Structural highlights
FunctionVRPI_BPT7 Bacterial RNA polymerase inhibitor, which is expressed in the late stage of lytic development, is also essential for continuous synthesis of phage DNA and functions in the packaging of the viral genome into the mature phage particle. Publication Abstract from PubMedThe T7 phage-encoded small protein Gp2 is a non-DNA-binding transcription factor that interacts with the jaw domain of the Escherichia coli (Ec) RNA polymerase (RNAp) beta' subunit and inhibits transcriptionally proficient promoter-complex (RPo) formation. Here, we describe the high-resolution solution structure of the Gp2-Ec beta' jaw domain complex and show that Gp2 and DNA compete for binding to the beta' jaw domain. We reveal that efficient inhibition of RPo formation by Gp2 requires the amino-terminal sigma(70) domain region 1.1 (R1.1), and that Gp2 antagonizes the obligatory movement of R1.1 during RPo formation. We demonstrate that Gp2 inhibits RPo formation not just by steric occlusion of the RNAp-DNA interaction but also through long-range antagonistic effects on RNAp-promoter interactions around the RNAp active center that likely occur due to repositioning of R1.1 by Gp2. The inhibition of Ec RNAp by Gp2 thus defines a previously uncharacterized mechanism by which bacterial transcription is regulated by a viral factor. Structural and Mechanistic Basis for the Inhibition of Escherichia coli RNA Polymerase by T7 Gp2.,James E, Liu M, Sheppard C, Mekler V, Camara B, Liu B, Simpson P, Cota E, Severinov K, Matthews S, Wigneshweraraj S Mol Cell. 2012 Jul 19. PMID:22819324[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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