Molecular dynamics study of the effect of active site protonation on Helicobacter pylori 5?-methylthioadenosine/S-adenosylhomocysteine nucleosidase
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Tarih
2015
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Springer Verlag
Erişim Hakkı
info:eu-repo/semantics/closedAccess
Özet
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 K2 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. © 2015, European Biophysical Societies' Association.
Açıklama
Anahtar Kelimeler
D198 protonation, Helicobacterpylori, Molecular dynamics simulation, MTAN
Kaynak
European Biophysics Journal
WoS Q Değeri
Scopus Q Değeri
Q2
Cilt
44
Sayı
8
