Structural highlights
Function
FTSZ_MYCTU Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells (By similarity). Binds GTP and shows GTPase activity.[HAMAP-Rule:MF_00909]
Publication Abstract from PubMed
The essential bacterial protein FtsZ is a guanosine triphosphatase that self-assembles into a structure at the division site termed the "Z ring". During cytokinesis, the Z ring exerts a constrictive force on the membrane by using the chemical energy of guanosine triphosphate hydrolysis. However, the structural basis of this constriction remains unresolved. Here, we present the crystal structure of a guanosine diphosphate-bound Mycobacterium tuberculosis FtsZ protofilament, which exhibits a curved conformational state. The structure reveals a longitudinal interface that is important for function. The protofilament curvature highlights a hydrolysis-dependent conformational switch at the T3 loop that leads to longitudinal bending between subunits, which could generate sufficient force to drive cytokinesis.
FtsZ protofilaments use a hinge-opening mechanism for constrictive force generation.,Li Y, Hsin J, Zhao L, Cheng Y, Shang W, Huang KC, Wang HW, Ye S Science. 2013 Jul 26;341(6144):392-5. doi: 10.1126/science.1239248. PMID:23888039[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Li Y, Hsin J, Zhao L, Cheng Y, Shang W, Huang KC, Wang HW, Ye S. FtsZ protofilaments use a hinge-opening mechanism for constrictive force generation. Science. 2013 Jul 26;341(6144):392-5. doi: 10.1126/science.1239248. PMID:23888039 doi:10.1126/science.1239248
