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- Title
Molecular dynamics study of the effect of active site protonation on Helicobacter pylori 5′-methylthioadenosine/ S-adenosylhomocysteine nucleosidase.
- Authors
Tekpinar, Mustafa; Yildirim, Ahmet; Wassenaar, Tsjerk
- Abstract
The protein 5′-methylthioadenosine/ S-adenosylhomocysteine nucleosidase (MTAN) is involved in the quorum sensing of several bacterial species, including Helicobacter pylori. In particular, these bacteria depend on MTAN for synthesis of vitamin K homologs. The residue D198 in the active site of MTAN seems to be of crucial importance, by acting as a hydrogen-bond acceptor for the ligand. In this study, we investigated the conformation and dynamics of apo and holo H. pylori MTAN ( HpMTAN), and assessed the effect of protonation of D198 by use of molecular dynamics simulations. Our results show that protonation of the active site of HpMTAN can cause a conformational transition from a closed state to an open state even in the absence of substrate, via inter-chain mechanical coupling.
- Subjects
MOLECULAR dynamics; BINDING sites; PROTON transfer reactions; HELICOBACTER pylori; METHYLTHIOADENOSINE; ADENOSYLHOMOCYSTEINE; NUCLEOSIDASES; QUORUM sensing
- Publication
European Biophysics Journal, 2015, Vol 44, Issue 8, p685
- ISSN
0175-7571
- Publication type
Article
- DOI
10.1007/s00249-015-1067-0