| Literature DB >> 24746687 |
Junso Fujita1, Yoko Maeda1, Chioko Nagao2, Yuko Tsuchiya2, Yuma Miyazaki1, Mika Hirose3, Eiichi Mizohata1, Yoshimi Matsumoto4, Tsuyoshi Inoue1, Kenji Mizuguchi2, Hiroyoshi Matsumura5.
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.Entities:
Keywords: Bacterial divisome; FtsA; FtsZ; Staphylococcus aureus
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Year: 2014 PMID： 24746687 DOI： 10.1016/j.febslet.2014.04.008
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124