Molecular dynamics study of the effect of active site protonation on Helicobacter pylori 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase

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dc.contributor.authorTekpinar, Mustafa
dc.contributor.authorYildirim, Ahmet
dc.contributor.authorA. Wassenaar, Tsjerk
dc.date.accessioned2019-11-28T10:50:37Z
dc.date.available2019-11-28T10:50:37Z
dc.date.issued2015en_US
dc.departmentFen - Edebiyat Fakültesien_US
dc.description.abstractThe 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.en_US
dc.description.provenanceSubmitted by Ahmet Yıldırım (ahmedoyildirim@siirt.edu.tr) on 2019-11-28T10:50:37Z No. of bitstreams: 1 11.pdf: 5312238 bytes, checksum: a2fb201480639e48eff7754e0ff9fe8d (MD5)en
dc.description.provenanceMade available in DSpace on 2019-11-28T10:50:37Z (GMT). No. of bitstreams: 1 11.pdf: 5312238 bytes, checksum: a2fb201480639e48eff7754e0ff9fe8d (MD5) Previous issue date: 2015en
dc.identifier.pmid26254213
dc.identifier.urihttps://hdl.handle.net/20.500.12604/1881
dc.identifier.wosWOS:000363952200009
dc.identifier.wosqualityQ4
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakPubMed
dc.institutionauthorYildirim, Ahmet
dc.language.isootheren_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.snmzKG_20241224
dc.titleMolecular dynamics study of the effect of active site protonation on Helicobacter pylori 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidaseen_US
dc.typeArticleen_US

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