22hq

Crystal structure of GDP-bound FtsZ from Acinetobacter baumannii

spinqualitylabelsall models 22hq, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 22hq is a 4 chain structure with sequence from Acinetobacter baumannii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Ligands: GDP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Acinetobacter baumannii is an opportunistic pathogen known for its extensive antibiotic resistance, posing a significant concern in healthcare settings. Given global concern over broad-spectrum antibiotic use and its impact on the human microbiome, targeting the bacterial cell-division protein Filamenting temperature-sensitive Z (FtsZ) is a promising strategy for developing new antibiotics, as this protein is essential for bacterial cell division. FtsZ polymerizes into filaments to form the Z-ring at the cell division site. This Z-ring orchestrates the recruitment of other crucial proteins in cytokinesis and cell wall synthesis, making it critical for bacterial viability. To target FtsZ from Acinetobacter baumannii (abFtsZ), we have elucidated the first crystal structures in the apo and GDP-bound state. The structural analysis revealed that the abFtsZ-GDP complex exists in a relaxed state conformation with weak inter-subunit interactions. The GTPase activity of abFtsZ showed a V(max) of 3.3 +/- 0.4 nmolP/nmolFtsZ/min, and a K(m) of 2.3 mM. By virtual screening using the crystal structure of abFtsZ, we identified six potential inhibitors: Gossypin, Stafib-1, Tryphostin A51, Sangivamycin, Scutellarin, and Ellagic acid that target the GTP-binding pocket. These inhibitors exhibited high docking scores ranging from -10.2 to -8.4 kcal/mol and remained stable throughout the 500 ns MD simulation. These inhibitors can serve as lead molecules for the development of a new antibacterial agent. Crystal structure of FtsZ from Acinetobacter baumannii and identification of a potential inhibitor targeting its GTPase domain.,Yadav AK, Naz F, Singh A, Sharma S, Deka J, Madhuri M, Saini C, Kumar M, Kaur P, Singh TP, Ethayathulla AS Int J Biol Macromol. 2026 May;364:152295. doi: 10.1016/j.ijbiomac.2026.152295. , Epub 2026 Apr 30. PMID:42067083 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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