Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6YM1

Mycobacterium tuberculosis FtsZ in complex with GDP

Summary for 6YM1
Entry DOI10.2210/pdb6ym1/pdb
DescriptorCell division protein FtsZ, GUANOSINE-5'-DIPHOSPHATE (3 entities in total)
Functional Keywordscell division protein, antibiotic
Biological sourceMycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Total number of polymer chains2
Total formula weight64411.47
Authors
Alnami, A.T.,Norton, R.S.,Pena, H.P.,Haider, M.,kozielski, F. (deposition date: 2020-04-07, release date: 2021-04-14, Last modification date: 2024-01-24)
Primary citationAlnami, A.,Norton, R.S.,Pena, H.P.,Haider, S.,Kozielski, F.
Conformational Flexibility of A Highly Conserved Helix Controls Cryptic Pocket Formation in FtsZ.
J.Mol.Biol., 433:167061-167061, 2021
Cited by
PubMed Abstract: Mycobacterium tuberculosis is responsible for more than 1.6 million deaths each year. One potential antibacterial target in M. tuberculosis is filamentous temperature sensitive protein Z (FtsZ), which is the bacterial homologue of mammalian tubulin, a validated cancer target. M. tuberculosis FtsZ function is essential, with its inhibition leading to arrest of cell division, elongation of the bacterial cell and eventual cell death. However, the development of potent inhibitors against FtsZ has been a challenge owing to the lack of structural information. Here we report multiple crystal structures of M. tuberculosis FtsZ in complex with a coumarin analogue. The 4-hydroxycoumarin binds exclusively to two novel cryptic pockets in nucleotide-free FtsZ, but not to the binary FtsZ-GTP or GDP complexes. Our findings provide a detailed understanding of the molecular basis for cryptic pocket formation, controlled by the conformational flexibility of the H7 helix, and thus reveal an important structural and mechanistic rationale for coumarin antibacterial activity.
PubMed: 34023403
DOI: 10.1016/j.jmb.2021.167061
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.7 Å)
Structure validation

227344

PDB entries from 2024-11-13

PDB statisticsPDBj update infoContact PDBjnumon