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Crystal structure of the Escherichia coli transcription termination factor Rho

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 o...

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Autores principales: Fan, Chengcheng, Rees, Douglas C.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7470046/
https://www.ncbi.nlm.nih.gov/pubmed/32880587
http://dx.doi.org/10.1107/S2053230X20010572
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author Fan, Chengcheng
Rees, Douglas C.
author_facet Fan, Chengcheng
Rees, Douglas C.
author_sort Fan, Chengcheng
collection PubMed
description 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; NaAtm1), it preferentially crystallized in space group C2 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 NaAtm1 preparation.
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spelling pubmed-74700462020-09-15 Crystal structure of the Escherichia coli transcription termination factor Rho Fan, Chengcheng Rees, Douglas C. Acta Crystallogr F Struct Biol Commun Research Communications 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; NaAtm1), it preferentially crystallized in space group C2 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 NaAtm1 preparation. International Union of Crystallography 2020-08-20 /pmc/articles/PMC7470046/ /pubmed/32880587 http://dx.doi.org/10.1107/S2053230X20010572 Text en © Fan & Rees 2020 http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.http://creativecommons.org/licenses/by/4.0/
spellingShingle Research Communications
Fan, Chengcheng
Rees, Douglas C.
Crystal structure of the Escherichia coli transcription termination factor Rho
title Crystal structure of the Escherichia coli transcription termination factor Rho
title_full Crystal structure of the Escherichia coli transcription termination factor Rho
title_fullStr Crystal structure of the Escherichia coli transcription termination factor Rho
title_full_unstemmed Crystal structure of the Escherichia coli transcription termination factor Rho
title_short Crystal structure of the Escherichia coli transcription termination factor Rho
title_sort crystal structure of the escherichia coli transcription termination factor rho
topic Research Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7470046/
https://www.ncbi.nlm.nih.gov/pubmed/32880587
http://dx.doi.org/10.1107/S2053230X20010572
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