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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...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
International Union of Crystallography
2020
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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. |
format | Online Article Text |
id | pubmed-7470046 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
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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