5MN5

S. aureus FtsZ 12-316 T66W GTP Closed form (2TCm)

Summary for 5MN5

• Entry DOI: 10.2210/pdb5mn5/pdb
• Descriptor: Cell division protein FtsZ, GUANOSINE-5'-TRIPHOSPHATE (2 entities in total)
• Functional Keywords: bacterial cell division, bacterial cytoskeleton, filamentous, gtpase, hydrolase
• Biological source: Staphylococcus aureus
• Cellular location: Cytoplasm : P0A031
• Total number of polymer chains: 2
• Total formula weight: 64269.84

Authors

Wagstaff, J.M.,Tsim, M.,Kureisaite-Ciziene, D.,Lowe, J. (deposition date: 2016-12-12, release date: 2016-12-21, Last modification date: 2024-01-17)

Primary citation

Wagstaff, J.M.,Tsim, M.,Oliva, M.A.,Garcia-Sanchez, A.,Kureisaite-Ciziene, D.,Andreu, J.M.,Lowe, J.
A Polymerization-Associated Structural Switch in FtsZ That Enables Treadmilling of Model Filaments.
MBio, 8:-, 2017

PubMed Abstract: Bacterial cell division in many organisms involves a constricting cytokinetic ring that is orchestrated by the tubulin-like protein FtsZ. FtsZ forms dynamic filaments close to the membrane at the site of division that have recently been shown to treadmill around the division ring, guiding septal wall synthesis. Here, using X-ray crystallography of FtsZ (SaFtsZ), we reveal how an FtsZ can adopt two functionally distinct conformations, open and closed. The open form is found in SaFtsZ filaments formed in crystals and also in soluble filaments of FtsZ as deduced by electron cryomicroscopy. The closed form is found within several crystal forms of two nonpolymerizing SaFtsZ mutants and corresponds to many previous FtsZ structures from other organisms. We argue that FtsZ's conformational switch is polymerization-associated, driven by the formation of the longitudinal intersubunit interfaces along the filament. We show that such a switch provides explanations for both how treadmilling may occur within a single-stranded filament and why filament assembly is cooperative. The FtsZ protein is a key molecule during bacterial cell division. FtsZ forms filaments that organize cell membrane constriction, as well as remodeling of the cell wall, to divide cells. FtsZ functions through nucleotide-driven filament dynamics that are poorly understood at the molecular level. In particular, mechanisms for cooperative assembly (nonlinear dependency on concentration) and treadmilling (preferential growth at one filament end and loss at the other) have remained elusive. Here, we show that most likely all FtsZ proteins have two distinct conformations, a "closed" form in monomeric FtsZ and an "open" form in filaments. The conformational switch that occurs upon polymerization explains cooperativity and, in concert with polymerization-dependent nucleotide hydrolysis, efficient treadmilling of FtsZ polymers.

PubMed: 28465423
DOI: 10.1128/mBio.00254-17

Experimental method

X-RAY DIFFRACTION (2.802 Å)