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Structural insight into the interaction of O-acetylserine sulfhydrylase with competitive, peptidic inhibitors by saturation transfer difference-NMR.

Authors :
Benoni R
Pertinhez TA
Spyrakis F
Davalli S
Pellegrino S
Paredi G
Pezzotti A
Bettati S
Campanini B
Mozzarelli A
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.)

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