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PDBsum entry 3vpa
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References listed in PDB file
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Key reference
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Title
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Structural reorganization of the bacterial cell-Division protein ftsz from staphylococcus aureus.
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Authors
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T.Matsui,
J.Yamane,
N.Mogi,
H.Yamaguchi,
H.Takemoto,
M.Yao,
I.Tanaka.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2012,
68,
1175-1188.
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PubMed id
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Abstract
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FtsZ is a key molecule in bacterial cell division. In the presence of GTP, it
polymerizes into tubulin-like protofilaments 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.
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