Abstract
The bacterial cell-division protein FtsA anchors FtsZ to the cytoplasmic membrane. But how FtsA and FtsZ interact during membrane division remains obscure. We have solved 2.2 Å resolution crystal structure for FtsA from Staphylococcus aureus. In the crystals, SaFtsA molecules within the dimer units are twisted, in contrast to the straight filament of FtsA from Thermotoga maritima, and the half of S12-S13 hairpin regions are disordered. We confirmed that SaFtsZ and SaFtsA associate in vitro, and found that SaFtsZ GTPase activity is enhanced by interaction with SaFtsA.
Keywords:
Bacterial divisome; FtsA; FtsZ; Staphylococcus aureus.
Copyright © 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacterial Proteins / chemistry*
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism
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Cell Division
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Crystallography, X-Ray
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Cytoskeletal Proteins / chemistry
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Cytoskeletal Proteins / genetics
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Cytoskeletal Proteins / metabolism
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Escherichia coli / genetics
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GTP Phosphohydrolases / chemistry
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GTP Phosphohydrolases / genetics
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GTP Phosphohydrolases / metabolism
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Models, Molecular
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Protein Binding
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Protein Multimerization*
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Protein Structure, Secondary*
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Protein Structure, Tertiary*
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
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Staphylococcus aureus / genetics
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Staphylococcus aureus / metabolism*
Substances
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Bacterial Proteins
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Cytoskeletal Proteins
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FtsA protein, Bacteria
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FtsZ protein, Bacteria
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Recombinant Proteins
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GTP Phosphohydrolases