5ZUE

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

Summary for 5ZUE

• Entry DOI: 10.2210/pdb5zue/pdb
• Descriptor: Cell division protein FtsZ, GUANOSINE-5'-TRIPHOSPHATE (2 entities in total)
• Functional Keywords: ftsz, gtpase, bacterial cell division, cytosolic protein
• Biological source: Mycobacterium tuberculosis H37Rv
• Total number of polymer chains: 1
• Total formula weight: 39279.89

Authors

Guan, F.,Yu, J.,Yu, J.,Liu, Y.,Li, Y.,Feng, X.H.,Huang, K.C.,Chang, Z.,Ye, S. (deposition date: 2018-05-07, release date: 2018-07-04, Last modification date: 2024-03-27)

Primary citation

Guan, F.,Yu, J.,Yu, J.,Liu, Y.,Li, Y.,Feng, X.H.,Huang, K.C.,Chang, Z.,Ye, S.
Lateral interactions between protofilaments of the bacterial tubulin homolog FtsZ are essential for cell division
Elife, 7:-, 2018

PubMed Abstract: The prokaryotic tubulin homolog FtsZ polymerizes into protofilaments, which further assemble into higher-order structures at future division sites to form the Z-ring, a dynamic structure essential for bacterial cell division. The precise nature of interactions between FtsZ protofilaments that organize the Z-ring and their physiological significance remain enigmatic. In this study, we solved two crystallographic structures of a pair of FtsZ protofilaments, and demonstrated that they assemble in an antiparallel manner through the formation of two different inter-protofilament lateral interfaces. Our in vivo photocrosslinking studies confirmed that such lateral interactions occur in living cells, and disruption of the lateral interactions rendered cells unable to divide. The inherently weak lateral interactions enable FtsZ protofilaments to self-organize into a dynamic Z-ring. These results have fundamental implications for our understanding of bacterial cell division and for developing antibiotics that target this key process.

PubMed: 29889022
DOI: 10.7554/eLife.35578

Experimental method

X-RAY DIFFRACTION (2.7 Å)