2p7v

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2p7v, resolution 2.600Å

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Crystal structure of the Escherichia coli regulator of sigma 70, Rsd, in complex with sigma 70 domain 4

Overview

The Escherichia coli Rsd protein binds tightly and specifically to the RNA, polymerase (RNAP) sigma(70) factor. Rsd plays a role in alternative sigma, factor-dependent transcription by biasing the competition between, sigma(70) and alternative sigma factors for the available core RNAP. Here, we determined the 2.6 A-resolution X-ray crystal structure of Rsd bound to, sigma(70) domain 4 (sigma(70)(4)), the primary determinant for Rsd binding, within sigma(70). The structure reveals that Rsd binding interferes with, the two primary functions of sigma(70)(4), core RNAP binding and promoter, -35 element binding. Interestingly, the most highly conserved Rsd residues, form a network of interactions through the middle of the Rsd structure, that connect the sigma(70)(4)-binding surface with three cavities exposed, on distant surfaces of Rsd, suggesting functional coupling between, sigma(70)(4) binding and other binding surfaces of Rsd, either for other, proteins or for as yet unknown small molecule effectors. These results, provide a structural basis for understanding the role of Rsd, as well as, its ortholog, AlgQ, a positive regulator of Pseudomonas aeruginosa, virulence, in transcription regulation.

About this Structure

2P7V is a Protein complex structure of sequences from Escherichia coli with MG as ligand. Full crystallographic information is available from OCA.

Reference

Crystal Structure of the Escherichia coli Regulator of sigma(70), Rsd, in Complex with sigma(70) Domain 4., Patikoglou GA, Westblade LF, Campbell EA, Lamour V, Lane WJ, Darst SA, J Mol Biol. 2007 Jul 3;. PMID:17681541

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