Nogueira, Maria Luiza C.
Sforca, Mauricio Luis
Chin, Yanni K. -Y.
Gorbatyuk, Vitaliy Y.
Robson, Scott A.
King, Glenn F.
Gueiros-Filho, Frederico J.
de Mattos Zeri, Ana Carolina
Número total de Autores: 10
Afiliação do(s) autor(es):
 Brazilian Biosci Natl Lab LNBio CNPEM, Campinas - Brazil
 Univ Queensland, Inst Mol Biosci, Brisbane, Qld - Australia
 Univ Queensland, Ctr Adv Imaging, Brisbane, Qld - Australia
 Genzyme Sanofi US, Bioanalyt Sci DSAR Clin Lab Sci, Framingham, MA - USA
 Harvard Univ, Sch Med, Dept Biol Chem & Mol Pharmacol, Boston, MA 02115 - USA
 Univ Sao Paulo, Dept Bioquim, IQ, Sao Paulo - Brazil
Número total de Afiliações: 7
Tipo de documento:
BIOMOLECULAR NMR ASSIGNMENTS;
Citações Web of Science:
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 (NH)-N-15-H-2-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. (AU)