Structure Guided Design of Biotin Protein Ligase Inhibitors for Antibiotic Discovery

2013 ◽  
Vol 14 (1) ◽  
pp. 4-20 ◽  
Author(s):  
Ashleigh Paparella ◽  
Tatiana Soares da Costa ◽  
Min Yap ◽  
William Tieu ◽  
Matthew Wilce ◽  
...  
2021 ◽  
Author(s):  
Xuejiao Song ◽  
Sarah K Henke ◽  
John E. Cronan

2021 ◽  
Vol 2021 ◽  
pp. 1-30
Author(s):  
Najwan Jubair ◽  
Mogana Rajagopal ◽  
Sasikala Chinnappan ◽  
Norhayati Binti Abdullah ◽  
Ayesha Fatima

Microbial resistance has progressed rapidly and is becoming the leading cause of death globally. The spread of antibiotic-resistant microorganisms has been a significant threat to the successful therapy against microbial infections. Scientists have become more concerned about the possibility of a return to the pre-antibiotic era. Thus, searching for alternatives to fight microorganisms has become a necessity. Some bacteria are naturally resistant to antibiotics, while others acquire resistance mainly by the misuse of antibiotics and the emergence of new resistant variants through mutation. Since ancient times, plants represent the leading source of drugs and alternative medicine for fighting against diseases. Plants are rich sources of valuable secondary metabolites, such as alkaloids, quinones, tannins, terpenoids, flavonoids, and polyphenols. Many studies focus on plant secondary metabolites as a potential source for antibiotic discovery. They have the required structural properties and can act by different mechanisms. This review analyses the antibiotic resistance strategies produced by multidrug-resistant bacteria and explores the phytochemicals from different classes with documented antimicrobial action against resistant bacteria, either alone or in combination with traditional antibiotics.


1998 ◽  
Vol 3 (12) ◽  
pp. 564-566 ◽  
Author(s):  
James R Brown ◽  
Patrick V Warren
Keyword(s):  

2021 ◽  
Vol 77 (4) ◽  
pp. 510-521
Author(s):  
Manoj Kumar Rajak ◽  
Sonika Bhatnagar ◽  
Shubhant Pandey ◽  
Sunil Kumar ◽  
Shalini Verma ◽  
...  

Biotin protein ligase catalyses the post-translational modification of biotin carboxyl carrier protein (BCCP) domains, a modification that is crucial for the function of several carboxylases. It is a two-step process that results in the covalent attachment of biotin to the ɛ-amino group of a conserved lysine of the BCCP domain of a carboxylase in an ATP-dependent manner. In Leishmania, three mitochondrial enzymes, acetyl-CoA carboxylase, methylcrotonyl-CoA carboxylase and propionyl-CoA carboxylase, depend on biotinylation for activity. In view of the indispensable role of the biotinylating enzyme in the activation of these carboxylases, crystal structures of L. major biotin protein ligase complexed with biotin and with biotinyl-5′-AMP have been solved. L. major biotin protein ligase crystallizes as a unique dimer formed by cross-handshake interactions of the hinge region of the two monomers formed by partial unfolding of the C-terminal domain. Interestingly, the substrate (BCCP domain)-binding site of each monomer is occupied by its own C-terminal domain in the dimer structure. This was observed in all of the crystals that were obtained, suggesting a closed/inactive conformation of the enzyme. Size-exclusion chromatography studies carried out using high protein concentrations (0.5 mM) suggest the formation of a concentration-dependent dimer that exists in equilibrium with the monomer.


Author(s):  
Sadhana Sagar ◽  
Shilpa Kaistha ◽  
Amar Jyoti Das ◽  
Rajesh Kumar
Keyword(s):  

2019 ◽  
Vol 45 (3) ◽  
pp. 255-277 ◽  
Author(s):  
Ellis C. O’Neill ◽  
Michelle Schorn ◽  
Charles B. Larson ◽  
Natalie Millán-Aguiñaga

2019 ◽  
Vol 53 (4) ◽  
pp. 371-382 ◽  
Author(s):  
Guillaume André Durand ◽  
Didier Raoult ◽  
Grégory Dubourg
Keyword(s):  

Sign in / Sign up

Export Citation Format

Share Document