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Crystal structure of FtsA from Staphylococcus aureus
Author(s) -
Fujita Junso,
Maeda Yoko,
Nagao Chioko,
Tsuchiya Yuko,
Miyazaki Yuma,
Hirose Mika,
Mizohata Eiichi,
Matsumoto Yoshimi,
Inoue Tsuyoshi,
Mizuguchi Kenji,
Matsumura Hiroyoshi
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.04.008
Subject(s) - ftsz , thermotoga maritima , dimer , biophysics , gtpase , cytoplasm , crystallography , protein filament , biology , cell division , staphylococcus aureus , chemistry , bacteria , microbiology and biotechnology , biochemistry , cell , escherichia coli , genetics , organic chemistry , gene
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.