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High-resolution crystal structures of Escherichia coli FtsZ bound to GDP and GTP
Bacterial cytokinesis is mediated by the Z-ring, which is formed by the prokaryotic tubulin homolog FtsZ. Recent data indicate that the Z-ring is composed of small patches of FtsZ protofilaments that travel around the bacterial cell by treadmilling. Treadmilling involves a switch from a relaxed (R)...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
International Union of Crystallography
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7010359/ https://www.ncbi.nlm.nih.gov/pubmed/32039891 http://dx.doi.org/10.1107/S2053230X20001132 |
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author | Schumacher, Maria A. Ohashi, Tomoo Corbin, Lauren Erickson, Harold P. |
author_facet | Schumacher, Maria A. Ohashi, Tomoo Corbin, Lauren Erickson, Harold P. |
author_sort | Schumacher, Maria A. |
collection | PubMed |
description | Bacterial cytokinesis is mediated by the Z-ring, which is formed by the prokaryotic tubulin homolog FtsZ. Recent data indicate that the Z-ring is composed of small patches of FtsZ protofilaments that travel around the bacterial cell by treadmilling. Treadmilling involves a switch from a relaxed (R) state, favored for monomers, to a tense (T) conformation, which is favored upon association into filaments. The R conformation has been observed in numerous monomeric FtsZ crystal structures and the T conformation in Staphylococcus aureus FtsZ crystallized as assembled filaments. However, while Escherichia coli has served as a main model system for the study of the Z-ring and the associated divisome, a structure has not yet been reported for E. coli FtsZ. To address this gap, structures were determined of the E. coli FtsZ mutant FtsZ(L178E) with GDP and GTP bound to 1.35 and 1.40 Å resolution, respectively. The E. coli FtsZ(L178E) structures both crystallized as straight filaments with subunits in the R conformation. These high-resolution structures can be employed to facilitate experimental cell-division studies and their interpretation in E. coli. |
format | Online Article Text |
id | pubmed-7010359 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
spelling | pubmed-70103592020-03-06 High-resolution crystal structures of Escherichia coli FtsZ bound to GDP and GTP Schumacher, Maria A. Ohashi, Tomoo Corbin, Lauren Erickson, Harold P. Acta Crystallogr F Struct Biol Commun Research Communications Bacterial cytokinesis is mediated by the Z-ring, which is formed by the prokaryotic tubulin homolog FtsZ. Recent data indicate that the Z-ring is composed of small patches of FtsZ protofilaments that travel around the bacterial cell by treadmilling. Treadmilling involves a switch from a relaxed (R) state, favored for monomers, to a tense (T) conformation, which is favored upon association into filaments. The R conformation has been observed in numerous monomeric FtsZ crystal structures and the T conformation in Staphylococcus aureus FtsZ crystallized as assembled filaments. However, while Escherichia coli has served as a main model system for the study of the Z-ring and the associated divisome, a structure has not yet been reported for E. coli FtsZ. To address this gap, structures were determined of the E. coli FtsZ mutant FtsZ(L178E) with GDP and GTP bound to 1.35 and 1.40 Å resolution, respectively. The E. coli FtsZ(L178E) structures both crystallized as straight filaments with subunits in the R conformation. These high-resolution structures can be employed to facilitate experimental cell-division studies and their interpretation in E. coli. International Union of Crystallography 2020-02-05 /pmc/articles/PMC7010359/ /pubmed/32039891 http://dx.doi.org/10.1107/S2053230X20001132 Text en © Schumacher et al. 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 Schumacher, Maria A. Ohashi, Tomoo Corbin, Lauren Erickson, Harold P. High-resolution crystal structures of Escherichia coli FtsZ bound to GDP and GTP |
title | High-resolution crystal structures of Escherichia coli FtsZ bound to GDP and GTP |
title_full | High-resolution crystal structures of Escherichia coli FtsZ bound to GDP and GTP |
title_fullStr | High-resolution crystal structures of Escherichia coli FtsZ bound to GDP and GTP |
title_full_unstemmed | High-resolution crystal structures of Escherichia coli FtsZ bound to GDP and GTP |
title_short | High-resolution crystal structures of Escherichia coli FtsZ bound to GDP and GTP |
title_sort | high-resolution crystal structures of escherichia coli ftsz bound to gdp and gtp |
topic | Research Communications |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7010359/ https://www.ncbi.nlm.nih.gov/pubmed/32039891 http://dx.doi.org/10.1107/S2053230X20001132 |
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