6LL5

Crystal structure of KpFtsZ (residues 11-316)

Summary for 6LL5

• Entry DOI: 10.2210/pdb6ll5/pdb
• Descriptor: Cell division protein FtsZ, GUANOSINE-5'-DIPHOSPHATE, GLYCEROL, ... (4 entities in total)
• Functional Keywords: cell dividsion, klebsiella pneumonie, cell cycle
• Biological source: Klebsiella pneumoniae
• Total number of polymer chains: 1
• Total formula weight: 32348.40

Authors

Yoshizawa, T.,Fujita, J.,Terakado, H.,Ozawa, M.,Kuroda, N.,Tanaka, S.,Uehara, R.,Matsumura, H. (deposition date: 2019-12-21, release date: 2020-02-26, Last modification date: 2023-11-22)

Primary citation

Yoshizawa, T.,Fujita, J.,Terakado, H.,Ozawa, M.,Kuroda, N.,Tanaka, S.I.,Uehara, R.,Matsumura, H.
Crystal structures of the cell-division protein FtsZ from Klebsiella pneumoniae and Escherichia coli.
Acta Crystallogr.,Sect.F, 76:86-93, 2020

PubMed Abstract: FtsZ, a tubulin-like GTPase, is essential for bacterial cell division. In the presence of GTP, FtsZ polymerizes into filamentous structures, which are key to generating force in cell division. However, the structural basis for the molecular mechanism underlying FtsZ function remains to be elucidated. In this study, crystal structures of the enzymatic domains of FtsZ from Klebsiella pneumoniae (KpFtsZ) and Escherichia coli (EcFtsZ) were determined at 1.75 and 2.50 Å resolution, respectively. Both FtsZs form straight protofilaments in the crystals, and the two structures adopted relaxed (R) conformations. The T3 loop, which is involved in GTP/GDP binding and FtsZ assembly/disassembly, adopted a unique open conformation in KpFtsZ, while the T3 loop of EcFtsZ was partially disordered. The crystal structure of EcFtsZ can explain the results from previous functional analyses using EcFtsZ mutants.

PubMed: 32039890
DOI: 10.1107/S2053230X2000076X

Experimental method

X-RAY DIFFRACTION (1.75 Å)