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Crystal structure of the Escherichia coli transcription termination factor Rho
Author(s) -
Fan Chengcheng,
Rees Douglas C.
Publication year - 2020
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x20010572
Subject(s) - escherichia coli , atp binding cassette transporter , crystallography , crystal structure , chemistry , transporter , transcription (linguistics) , biochemistry , biophysics , biology , gene , linguistics , philosophy
During 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 ∼1% of the target protein (a bacterial homolog of the eukaryotic ABC transporter of mitochondria from Novosphingobium aromaticivorans ; Na Atm1), it preferentially crystallized in space group C 2 as thin plates that diffracted to 3.30 Å 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 Na Atm1 preparation.