1sg5

Solution structure of Yaeo, a Rho-specific inhibitor of transcription termination

spinqualitylabelsall models 1sg5 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1sg5 is a 1 chain structure with sequence from Escherichia coli. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN Function ROF_ECOLI Suppresses temperature-sensitive mutations in essential genes by modulating rho-dependent transcription termination. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Rho-dependent transcription termination is an essential process for the regulation of bacterial gene expression. Thus far, only two Rho-specific inhibitors of bacterial transcription termination have been described, the psu protein from the satellite bacteriophage P4 and YaeO from Escherichia coli. Here, we report the solution structure of YaeO, the first of a Rho-specific inhibitor of transcription termination. YaeO is an acidic protein composed of an N-terminal helix and a seven-stranded beta sandwich. NMR chemical shift perturbation experiments revealed that YaeO binds proximal to the primary nucleic acid binding site of Rho. Based on the NMR titrations, a docked model of the YaeO-Rho complex was calculated. These results suggest that YaeO binds outside the Rho hexamer, acting as a competitive inhibitor of RNA binding. In vitro gel shift assays confirmed the inhibition of nucleic acid binding to Rho. Site-directed mutagenesis showed that the negative character of YaeO is essential for its function in vivo. Solution structure of YaeO, a Rho-specific inhibitor of transcription termination.,Gutierrez P, Kozlov G, Gabrielli L, Elias D, Osborne MJ, Gallouzi IE, Gehring K J Biol Chem. 2007 Aug 10;282(32):23348-53. Epub 2007 Jun 11. PMID:17565995 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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