title: FtsZ protofilaments use a hinge-opening mechanism for constrictive force generation.
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.
authors.affiliation: Life Sciences Institute, Zhejiang University, Hangzhou, 310058 Zhejiang, P.R. China.
authors.forename: Ying
authors.initials: Y
authors.lastname: Li
authors.forename: Jen
authors.initials: J
authors.lastname: Hsin
authors.forename: Lingyun
authors.initials: L
authors.lastname: Zhao
authors.forename: Yiwen
authors.initials: Y
authors.lastname: Cheng
authors.forename: Weina
authors.initials: W
authors.lastname: Shang
authors.forename: Kerwyn Casey
authors.initials: KC
authors.lastname: Huang
authors.forename: Hong-Wei
authors.initials: HW
authors.lastname: Wang
authors.forename: Sheng
authors.initials: S
authors.lastname: Ye
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D002462:Cell Membrane / Q000502:physiology; D018360:Crystallography, X-Ray; D048749:Cytokinesis; D003598:Cytoskeletal Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000737:chemistry; D006153:Guanosine Diphosphate / Q000737:chemistry / Q000378:metabolism; D006160:Guanosine Triphosphate / Q000378:metabolism; D006868:Hydrolysis; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D056004:Molecular Dynamics Simulation; D008969:Molecular Sequence Data; D009169:Mycobacterium tuberculosis / Q000737:chemistry* / Q000502:physiology; D017354:Point Mutation; D011487:Protein Conformation; D055503:Protein Multimerization; D021122:Protein Subunits / Q000737:chemistry / Q000378:metabolism; D013211:Staphylococcus aureus / Q000737:chemistry
chemical_list: D001426:Bacterial Proteins; D003598:Cytoskeletal Proteins; C071525:FtsZ protein, Bacteria; D021122:Protein Subunits; D006153:Guanosine Diphosphate; D006160:Guanosine Triphosphate