6ll5
Crystal structure of KpFtsZ (residues 11-316)Crystal structure of KpFtsZ (residues 11-316)
Structural highlights
FunctionA0A0H3GRR0_KLEPH Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity.[HAMAP-Rule:MF_00909][RuleBase:RU000631] Publication Abstract from PubMedFtsZ, 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 A 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. Crystal structures of the cell-division protein FtsZ from Klebsiella pneumoniae and Escherichia coli.,Yoshizawa T, Fujita J, Terakado H, Ozawa M, Kuroda N, Tanaka SI, Uehara R, Matsumura H Acta Crystallogr F Struct Biol Commun. 2020 Feb 1;76(Pt 2):86-93. doi:, 10.1107/S2053230X2000076X. Epub 2020 Feb 5. PMID:32039890[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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