5v68 | pdb_00005v68

Crystal structure of cell division protein FtsZ from Mycobacterium tuberculosis bounded via the T9 loop

spinqualitylabelsall models 5v68, resolution 3.46Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5v68 is a 6 chain structure with sequence from Mycobacterium tuberculosis H37Ra. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.46Å Ligands: GDP, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FTSZ_MYCTA 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 (By similarity). Binds GTP and shows GTPase activity.[HAMAP-Rule:MF_00909] Publication Abstract from PubMed As of 2017, tuberculosis had infected 1.7 billion people (23% of the population of the world) and caused ten million deaths. Mycobacterium tuberculosis (Mtb) is quickly evolving, and new strains are classified as multidrug resistant. Thus, the identification of novel druggable targets is essential to combat the proliferation of these drug-resistant strains. Filamenting temperature-sensitive mutant Z (FtsZ) is a key protein involved in cytokinesis, an important process for Mtb proliferation and viability. FtsZ is required for bacterial cell division because it polymerizes into a structure called the Z-ring, which recruits accessory division proteins to the septum. Here, the crystal structure of the MtbFtsZ protein has been determined to 3.46 A resolution and is described as a dimer of trimers, with an inter-subunit interface between protomers AB and DE. In this work, a novel conformation of MtbFtsZ is revealed involving the T9 loop and the nucleotide-binding pocket of protomers BC and EF. Novel T9 loop conformation of filamenting temperature-sensitive mutant Z from Mycobacterium tuberculosis.,Lazo EO, Jakoncic J, RoyChowdhury S, Awasthi D, Ojima I Acta Crystallogr F Struct Biol Commun. 2019 May 1;75(Pt 5):359-367. doi:, 10.1107/S2053230X19004618. Epub 2019 Apr 24. PMID:31045565 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cell division protein 3D structures Proteins from Mycobacterium tuberculosis

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