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Structural reorganization of the bacterial cell-division protein FtsZ from Staphylococcus aureus

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Title: Structural reorganization of the bacterial cell-division protein FtsZ from Staphylococcus aureus
Authors: Matsui, Takashi Browse this author
Yamane, Junji Browse this author
Mogi, Nobuyuki Browse this author
Yamaguchi, Hiroto Browse this author
Takemoto, Hiroshi Browse this author
Yao, Min Browse this author →KAKEN DB
Tanaka, Isao Browse this author →KAKEN DB
Keywords: FtsZ
tubulin
cell division
conformational change
inhibitor complex
Issue Date: Sep-2012
Publisher: International Union of Crystallography
Journal Title: Acta Crystallographica Section D: Biological Crystallography
Volume: 68
Issue: 9
Start Page: 1175
End Page: 1188
Publisher DOI: 10.1107/S0907444912022640
PMID: 22948918
Abstract: FtsZ is a key molecule in bacterial cell division. In the presence of GTP, it polymerizes into tubulin-like proto-filaments by head-to-tail association. Protofilaments of FtsZ seem to adopt a straight or a curved conformation in relation to the bound nucleotide. However, although several bacterial and archaeal FtsZ structures have been determined, all of the structures reported previously are considered to have a curved conformation. In this study, structures of FtsZ from Staphylococcus aureus (SaFtsZ) were determined in apo, GDP-bound and inhibitor-complex forms and it was found that SaFtsZ undergoes marked conformational changes. The accumulated evidence suggests that the GDP-bound structure has the features of the straight form. The structural change between the curved and straight forms shows intriguing similarity to the eukaryotic cytoskeletal protein tubulin. Furthermore, the structure of the apo form showed an unexpectedly large conformational change in the core region. FtsZ has also been recognized as a novel target for antibacterial drugs. The structure of the complex with the inhibitor PC190723, which has potent and selective antistaphylococcal activity, indicated that the inhibitor binds at the cleft between the two subdomains.
Type: article
URI: http://hdl.handle.net/2115/50282
Appears in Collections:生命科学院・先端生命科学研究院 (Graduate School of Life Science / Faculty of Advanced Life Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 田中 勲

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