2a8v

RHO TRANSCRIPTION TERMINATION FACTOR/RNA COMPLEX

spinqualitylabelsall models 2a8v, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2a8v is a 5 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, RCSB, PDBsum 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 The E. coli Rho protein disengages newly transcribed RNA from its DNA template, helping terminate certain transcripts. We have determined the X-ray crystal structure of the RNA-binding domain of Rho complexed to an RNA ligand. Filters that screen both ligand size and chemical functionality line the primary nucleic acid-binding site, imparting sequence specificity to a generic single-stranded nucleic acid-binding fold and explaining the preference of Rho for cytosine-rich RNA. The crystal packing reveals two Rho domain protomers bound to a single RNA with a single base spacer, suggesting that the strong RNA-binding sites of Rho may arise from pairing of RNA-binding modules. Dimerization of symmetric subunits on an asymmetric ligand is developed as a model for allosteric control in the action of the intact Rho hexamer. The structural basis for terminator recognition by the Rho transcription termination factor.,Bogden CE, Fass D, Bergman N, Nichols MD, Berger JM Mol Cell. 1999 Apr;3(4):487-93. PMID:10230401 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Helicase Transcription Termination Factor Rho

Proteopedia Page Contributors and Editors (what is this?)

OCA