High-resolution crystal structures of Escherichia coli FtsZ bound to GDP and GTP

Autor:	Maria A. Schumacher, Lauren C. Corbin, Tomoo Ohashi, Harold P. Erickson
Rok vydání:	2020
Předmět:	Models Molecular GTP' Protein Conformation Biophysics cytokinesis macromolecular substances Crystallography X-Ray medicine.disease_cause physiological processes FtsZ Guanosine Diphosphate Biochemistry Research Communications 03 medical and health sciences Protein structure Bacterial Proteins Structural Biology Z-ring protofilaments Escherichia coli Genetics medicine treadmilling Cytoskeleton 030304 developmental biology 0303 health sciences biology 030306 microbiology Chemistry Condensed Matter Physics Cytoskeletal Proteins Treadmilling Tubulin biology.protein bacteria Guanosine Triphosphate biological phenomena cell phenomena and immunity Cytokinesis
Zdroj:	Acta Crystallographica. Section F, Structural Biology Communications
ISSN:	2053-230X
DOI:	10.1107/s2053230x20001132
Popis:	Escherichia coli has served as the main model system for examining cell division in bacteria; however, the structure of the central cytokinesis protein FtsZ has not been determined to date. Here, high-resolution structures of E. coli FtsZ in GDP-bound and GTP-bound states are described. 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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b5455b45a3b95b51d7dae3c854286a6b https://doi.org/10.1107/s2053230x20001132 Zobrazit plný text záznamu Plný text ve formátu PDF Plný text ve formátu HTML
Nepřihlášeným uživatelům se plný text nezobrazuje	K zobrazení výsledku je třeba se přihlásit.