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8IBN

Cryo-EM structure of KpFtsZ single filament

Summary for 8IBN
Entry DOI10.2210/pdb8ibn/pdb
Related8GZV 8GZW 8GZX 8GZY 8H1O
EMDB information34429 35344
DescriptorCell division protein FtsZ, PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER, POTASSIUM ION (3 entities in total)
Functional Keywordsbacterial cell division, divisome, monobody, cell cycle
Biological sourceKlebsiella pneumoniae
Total number of polymer chains4
Total formula weight164540.93
Authors
Fujita, J.,Amesaka, H.,Yoshizawa, T.,Kuroda, N.,Kamimura, N.,Hibino, K.,Konishi, T.,Kato, Y.,Hara, M.,Inoue, T.,Namba, K.,Tanaka, S.,Matsumura, H. (deposition date: 2023-02-10, release date: 2023-08-02, Last modification date: 2024-05-08)
Primary citationFujita, J.,Amesaka, H.,Yoshizawa, T.,Hibino, K.,Kamimura, N.,Kuroda, N.,Konishi, T.,Kato, Y.,Hara, M.,Inoue, T.,Namba, K.,Tanaka, S.I.,Matsumura, H.
Structures of a FtsZ single protofilament and a double-helical tube in complex with a monobody.
Nat Commun, 14:4073-4073, 2023
Cited by
PubMed Abstract: FtsZ polymerizes into protofilaments to form the Z-ring that acts as a scaffold for accessory proteins during cell division. Structures of FtsZ have been previously solved, but detailed mechanistic insights are lacking. Here, we determine the cryoEM structure of a single protofilament of FtsZ from Klebsiella pneumoniae (KpFtsZ) in a polymerization-preferred conformation. We also develop a monobody (Mb) that binds to KpFtsZ and FtsZ from Escherichia coli without affecting their GTPase activity. Crystal structures of the FtsZ-Mb complexes reveal the Mb binding mode, while addition of Mb in vivo inhibits cell division. A cryoEM structure of a double-helical tube of KpFtsZ-Mb at 2.7 Å resolution shows two parallel protofilaments. Our present study highlights the physiological roles of the conformational changes of FtsZ in treadmilling that regulate cell division.
PubMed: 37429870
DOI: 10.1038/s41467-023-39807-5
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.03 Å)
Structure validation

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數據於2024-11-06公開中

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