| Affiliation: | 1.Brazilian Biosciences National Laboratory (LNBio-CNPEM),Campinas,Brazil;2.Departamento de Bioquímica, IQ,Universidade de S?o Paulo,S?o Paulo,Brazil;3.Institute for Molecular Bioscience,The University of Queensland,Brisbane,Australia;4.Centre for Advanced Imaging,The University of Queensland,Brisbane,Australia;5.BioNMR Facility, Biotechnology-Bioservices Center,University of Connecticut,Mansfield,USA;6.Bioanalytical Sciences DSAR Clinical Laboratory Sciences,Genzyme/Sanofi US,Framingham,USA;7.Department of Biological Chemistry and Molecular Pharmacology,Harvard Medical School,Boston,USA |
| Abstract: | Bacterial division begins with the formation of a contractile protein ring at midcell, which constricts the bacterial envelope to generate two daughter cells. The central component of the division ring is FtsZ, a tubulin-like protein capable of self-assembling into filaments which further associate into a higher order structure known as the Z ring. Proteins that bind to FtsZ play a crucial role in the formation and regulation of the Z ring. One such protein is ZapA, a widely conserved 21 kDa homodimeric protein that associates with FtsZ filaments and promotes their bundling. Although ZapA was discovered more than a decade ago, the structural details of its interaction with FtsZ remain unknown. In this work, backbone and side chain NMR assignments for the Geobacillus stearothermophilus ZapA homodimer are described. We titrated FtsZ into 15N2H-ZapA and mapped ZapA residues whose resonances are perturbed upon FtsZ binding. This information provides a structural understanding of the interaction between FtsZ and ZapA. |
