6Z0P

BceF Tyrosine Kinase Domain

Summary for 6Z0P

• Entry DOI: 10.2210/pdb6z0p/pdb
• Descriptor: BceF, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
• Functional Keywords: bacterial tyrosine kinase, bcef, biofilm, burkholderia cepacia, exopolysaccharide biosynthesis, transferase
• Biological source: Burkholderia cepacia
• Total number of polymer chains: 2
• Total formula weight: 59784.23

Authors

Landau, M.,Mayer, M.,Abd Alhadi, M.,Dvir, H. (deposition date: 2020-05-10, release date: 2021-04-14, Last modification date: 2024-01-24)

Primary citation

Mayer, M.,Matiuhin, Y.,Nawatha, M.,Tabachnikov, O.,Fish, I.,Schutz, N.,Dvir, H.,Landau, M.
Structural and Functional Insights into the Biofilm-Associated BceF Tyrosine Kinase Domain from Burkholderia cepacia .
Biomolecules, 11:-, 2021

PubMed Abstract: BceF is a bacterial tyrosine kinase (BY-kinase) from , a Gram-negative bacterium accountable for respiratory infections in immunocompromised and cystic fibrosis patients. BceF is involved in the production of exopolysaccharides secreted to the biofilm matrix and promotes resistant and aggressive infections. BY-kinases share no homology with mammalian kinases, and thereby offer a means to develop novel and specific antivirulence drugs. Here, we report the crystal structure of the BceF kinase domain at 1.85 Å resolution. The isolated BceF kinase domain is assembled as a dimer in solution and crystallized as a dimer in the asymmetric unit with endogenous adenosine-diphosphate bound at the active sites. The low enzymatic efficiency measured in solution may be explained by the partial obstruction of the active sites at the crystallographic dimer interface. This study provides insights into self-assembly and the specific activity of isolated catalytic domains. Several unique variations around the active site compared to other BY-kinases may allow for structure-based design of specific inhibitors to target virulence.

PubMed: 34439861
DOI: 10.3390/biom11081196

Experimental method

X-RAY DIFFRACTION (1.85 Å)