5H5H

Staphylococcus aureus FtsZ-GDP R29A mutant in T state

Summary for 5H5H

• Entry DOI: 10.2210/pdb5h5h/pdb
• Related: 5H5G 5H5I
• Descriptor: Cell division protein FtsZ, GUANOSINE-5'-DIPHOSPHATE, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: tubulin/ftsz family, gtpase, protofilament, cell cycle
• Biological source: Staphylococcus aureus (strain MRSA252)
• Cellular location: Cytoplasm : Q6GHP9
• Total number of polymer chains: 1
• Total formula weight: 32250.19

Authors

Fujita, J.,Harada, R.,Maeda, Y.,Saito, Y.,Mizohata, E.,Inoue, T.,Shigeta, Y.,Matsumura, H. (deposition date: 2016-11-05, release date: 2017-05-24, Last modification date: 2023-11-08)

Primary citation

Fujita, J.,Harada, R.,Maeda, Y.,Saito, Y.,Mizohata, E.,Inoue, T.,Shigeta, Y.,Matsumura, H.
Identification of the key interactions in structural transition pathway of FtsZ from Staphylococcus aureus
J. Struct. Biol., 198:65-73, 2017

PubMed Abstract: The tubulin-homolog protein FtsZ is essential for bacterial cell division. FtsZ polymerizes to form protofilaments that assemble into a contractile ring-shaped structure in the presence of GTP. Recent studies showed that FtsZ treadmilling coupled with the GTPase activity drives cell wall synthesis and bacterial cell division. The treadmilling caused by assembly and disassembly of FtsZ links to a conformational change of the monomer from a tense (T) to a relaxed (R) state, but considerable controversy still remains concerning the mechanism. In this study, we report crystal structures of FtsZ from Staphylococcus aureus corresponding to the T and R state conformations in the same crystal, indicating the structural equilibrium of the two state. The two structures identified a key residue Arg29, whose importance was also confirmed by our modified MD simulations. Crystal structures of the R29A mutant showed T and R state-like conformations with slight but important structural changes compared to those of wild-type. Collectively, these data provide new insights for understanding how intramolecular interactions are related to the structural transition of FtsZ.

PubMed: 28456664
DOI: 10.1016/j.jsb.2017.04.008

Experimental method

X-RAY DIFFRACTION (1.7 Å)