Open AccessCrystallization and preliminary X‐ray analysis of Psu, an inhibitor of the bacterial transcription terminator Rho
Author(s) -
Khamrui Susmita,
Ranjan Amitabh,
Pani Bibhusita,
Sen Ranjan,
Sen Udayaditya
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109053846
Subject(s) - dimer , crystallization , elongation , transcription (linguistics) , crystallography , in vivo , biophysics , terminator (solar) , rna , chemistry , bacteriophage , in vitro , microbiology and biotechnology , stereochemistry , biology , biochemistry , escherichia coli , physics , materials science , gene , genetics , organic chemistry , ionosphere , linguistics , philosophy , astronomy , metallurgy , ultimate tensile strength
Psu, a coat protein from bacteriophage P4, inhibits Rho‐dependent transcription termination both in vivo and in vitro . The Psu protein is α‐helical in nature and appeared to be a dimer in solution. It interacts with Rho and affects the ATP binding and RNA‐dependent ATPase activity of Rho, which in turn reduces the rate of RNA release from the elongation complex. Crystals of Psu were grown in space group I 422 in the presence of PEG, with unit‐cell parameters a = b = 148.76, c = 63.38 Å and a calculated Matthews coefficient of 2.1 Å 3 Da −1 (41.5% solvent content), assuming the presence of two molecules in the asymmetric unit. A native data set was collected to 2.3 Å resolution.