High-resolution crystal structures of Escherichia coli FtsZ bound to GDP and GTP.
Acta Crystallogr F Struct Biol Commun
; 76(Pt 2): 94-102, 2020 Feb 01.
Article
em En
| MEDLINE
| ID: mdl-32039891
ABSTRACT
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 1.40â
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.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Conformação Proteica
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Proteínas de Bactérias
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Proteínas do Citoesqueleto
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Escherichia coli
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Guanosina Difosfato
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Guanosina Trifosfato
Idioma:
En
Revista:
Acta Crystallogr F Struct Biol Commun
Ano de publicação:
2020
Tipo de documento:
Article
País de afiliação:
Estados Unidos