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Structural insight into the interaction of O-acetylserine sulfhydrylase with competitive, peptidic inhibitors by saturation transfer difference-NMR.
- Source :
-
FEBS letters [FEBS Lett] 2016 Apr; Vol. 590 (7), pp. 943-53. Date of Electronic Publication: 2016 Mar 22. - Publication Year :
- 2016
-
Abstract
- O-acetylserine sulfhydrylase (OASS), the enzyme catalysing the last step of cysteine biosynthesis in bacteria, is involved in antibiotic resistance and biofilm formation. Since mammals lack OASS, it is a potential target for antimicrobials. However, a limited number of inhibitors has been developed and crystallized in complex with OASS. STD-NMR was applied to study the interaction of the inhibitory pentapeptide MNYDI with the CysK and CysM OASS isozymes from Salmonella Typhimurium. Results are in excellent agreement with docking and SAR studies and confirm the important role played by the C-terminal Ile5 and the arylic moiety at P3 in dictating affinity.<br /> (© 2016 Federation of European Biochemical Societies.)
- Subjects :
- Anti-Bacterial Agents chemistry
Anti-Bacterial Agents metabolism
Antimicrobial Cationic Peptides chemistry
Antimicrobial Cationic Peptides metabolism
Antimicrobial Cationic Peptides pharmacology
Bacterial Proteins chemistry
Bacterial Proteins genetics
Bacterial Proteins metabolism
Binding Sites
Cysteine Synthase chemistry
Cysteine Synthase genetics
Cysteine Synthase metabolism
Enzyme Inhibitors chemistry
Enzyme Inhibitors metabolism
Epitope Mapping
Haemophilus influenzae enzymology
Hydrogen Bonding
Isoenzymes antagonists & inhibitors
Isoenzymes chemistry
Isoenzymes genetics
Isoenzymes metabolism
Molecular Docking Simulation
Nuclear Magnetic Resonance, Biomolecular
Oligopeptides chemistry
Oligopeptides metabolism
Peptide Library
Protein Conformation
Protein Interaction Domains and Motifs
Recombinant Proteins chemistry
Recombinant Proteins metabolism
Structural Homology, Protein
Anti-Bacterial Agents pharmacology
Bacterial Proteins antagonists & inhibitors
Cysteine Synthase antagonists & inhibitors
Enzyme Inhibitors pharmacology
Models, Molecular
Oligopeptides pharmacology
Salmonella typhimurium enzymology
Subjects
Details
- Language :
- English
- ISSN :
- 1873-3468
- Volume :
- 590
- Issue :
- 7
- Database :
- MEDLINE
- Journal :
- FEBS letters
- Publication Type :
- Academic Journal
- Accession number :
- 27072053
- Full Text :
- https://doi.org/10.1002/1873-3468.12126