5V68

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

Summary for 5V68

• Entry DOI: 10.2210/pdb5v68/pdb
• Descriptor: Cell division protein FtsZ, GUANOSINE-5'-DIPHOSPHATE, PHOSPHATE ION (3 entities in total)
• Functional Keywords: t9 loop, mtbftsz, phosphate, gdp, z-ring, cell cycle
• Biological source: Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)
• Total number of polymer chains: 6
• Total formula weight: 233820.72

Authors

Lazo, E.O.,Ojima, I.,Chowdhury, S.R.,Awasthi, D.,Jakoncic, J. (deposition date: 2017-03-16, release date: 2017-03-29, Last modification date: 2023-10-04)

Primary citation

Lazo, E.O.,Jakoncic, J.,RoyChowdhury, S.,Awasthi, D.,Ojima, I.
Novel T9 loop conformation of filamenting temperature-sensitive mutant Z from Mycobacterium tuberculosis.
Acta Crystallogr.,Sect.F, 75:359-367, 2019

PubMed Abstract: 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 Å 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.

PubMed: 31045565
DOI: 10.1107/S2053230X19004618

Experimental method

X-RAY DIFFRACTION (3.46 Å)