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Crystal structure of the E. coli transcription termination factor RhoCrystal structure of the E. coli transcription termination factor Rho
Structural highlights
FunctionRHO_ECOLI Facilitates transcription termination by a mechanism that involves rho binding to the nascent RNA, activation of rho's RNA-dependent ATPase activity, and release of the mRNA from the DNA template. RNA-dependent NTPAse which utilizes all four ribonucleoside triphosphates as substrates.[HAMAP-Rule:MF_01884] Publication Abstract from PubMedDuring the crystal structure analysis of an ATP-binding cassette (ABC) transporter overexpressed in Escherichia coli, a contaminant protein was crystallized. The identity of the contaminant was revealed by mass spectrometry to be the Escherichia coli transcription terminator factor Rho, structures of which had been previously determined in different conformational states. Although Rho was present at only approximately 1% of the target protein (a bacterial homolog of the eukaryotic ABC transporter of mitochondria from Novosphingobium aromaticivorans; NaAtm1), it preferentially crystallized in space group C2 as thin plates that diffracted to 3.30 A resolution. The structure of Rho in this crystal form exhibits a hexameric open-ring staircase conformation with bound ATP; this characteristic structure was also observed on electron-microscopy grids of the NaAtm1 preparation. Crystal structure of the Escherichia coli transcription termination factor Rho.,Fan C, Rees DC Acta Crystallogr F Struct Biol Commun. 2020 Sep 1;76(Pt 9):398-405. doi:, 10.1107/S2053230X20010572. Epub 2020 Aug 20. PMID:32880587[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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