4KWE

GDP-bound, double-stranded, curved FtsZ protofilament structure

Summary for 4KWE

• Entry DOI: 10.2210/pdb4kwe/pdb
• Descriptor: Cell division protein FtsZ, GUANOSINE-5'-DIPHOSPHATE (2 entities in total)
• Functional Keywords: rossmann fold, bacterial cell division, gtp-binding protein
• Biological source: Mycobacterium tuberculosis
• Cellular location: Cytoplasm (By similarity): P64170
• Total number of polymer chains: 3
• Total formula weight: 118548.62

Authors

Li, Y.,Hsin, J.,Zhao, L.,Cheng, Y.,Shang, W.,Huang, K.C.,Wang, H.W.,Ye, S. (deposition date: 2013-05-23, release date: 2013-07-31, Last modification date: 2024-03-20)

Primary citation

Li, Y.,Hsin, J.,Zhao, L.,Cheng, Y.,Shang, W.,Huang, K.C.,Wang, H.W.,Ye, S.
FtsZ protofilaments use a hinge-opening mechanism for constrictive force generation
Science, 341:392-395, 2013

PubMed Abstract: 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.

PubMed: 23888039
DOI: 10.1126/science.1239248

Experimental method

X-RAY DIFFRACTION (2.91 Å)