Structural highlights
Publication Abstract from PubMed
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 A 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.
Crystal structure of FtsA from Staphylococcus aureus.,Fujita J, Maeda Y, Nagao C, Tsuchiya Y, Miyazaki Y, Hirose M, Mizohata E, Matsumoto Y, Inoue T, Mizuguchi K, Matsumura H FEBS Lett. 2014 May 21;588(10):1879-85. doi: 10.1016/j.febslet.2014.04.008. Epub , 2014 Apr 18. PMID:24746687[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Fujita J, Maeda Y, Nagao C, Tsuchiya Y, Miyazaki Y, Hirose M, Mizohata E, Matsumoto Y, Inoue T, Mizuguchi K, Matsumura H. Crystal structure of FtsA from Staphylococcus aureus. FEBS Lett. 2014 May 21;588(10):1879-85. doi: 10.1016/j.febslet.2014.04.008. Epub , 2014 Apr 18. PMID:24746687 doi:http://dx.doi.org/10.1016/j.febslet.2014.04.008
