2MMV

ZapA mutant dimer from Geobacillus stearothermophilus

Summary for 2MMV

• Entry DOI: 10.2210/pdb2mmv/pdb
• NMR Information: BMRB: 19869
• Descriptor: Cell division protein ZapA (1 entity in total)
• Functional Keywords: zapa, cell cycle
• Biological source: Geobacillus stearothermophilus
• Cellular location: Cytoplasm : A0A078N0N2
• Total number of polymer chains: 2
• Total formula weight: 19804.86

Authors

Nogueira, M.L.,Sforca, M.,Zeri, A. (deposition date: 2014-03-19, release date: 2015-06-17, Last modification date: 2024-05-15)

Primary citation

Nogueira, M.L.,Sforca, M.L.,Chin, Y.K.,Mobli, M.,Handler, A.,Gorbatyuk, V.Y.,Robson, S.A.,King, G.F.,Gueiros-Filho, F.J.,Zeri, A.C.
Backbone and side chain NMR assignments of Geobacillus stearothermophilus ZapA allow identification of residues that mediate the interaction of ZapA with FtsZ.
Biomol.Nmr Assign., 9:387-391, 2015

PubMed 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 (15)N(2)H-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.

PubMed: 25967379
DOI: 10.1007/s12104-015-9615-1

Experimental method

SOLUTION NMR