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Dimerization of long hibernation promoting factor from Staphylococcus aureus: Structural analysis and biochemical characterization

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dc.contributor.author Usachev K.
dc.contributor.author Fatkhullin B.
dc.contributor.author Klochkova E.
dc.contributor.author Miftakhov A.
dc.contributor.author Golubev A.
dc.contributor.author Bikmullin A.
dc.contributor.author Nurullina L.
dc.contributor.author Garaeva N.
dc.contributor.author Islamov D.
dc.contributor.author Gabdulkhakov A.
dc.contributor.author Lekontseva N.
dc.contributor.author Tishchenko S.
dc.contributor.author Balobanov V.
dc.contributor.author Khusainov I.
dc.contributor.author Yusupov M.
dc.contributor.author Validov S.
dc.date.accessioned 2020-01-21T20:45:59Z
dc.date.available 2020-01-21T20:45:59Z
dc.date.issued 2019
dc.identifier.issn 1047-8477
dc.identifier.uri https://dspace.kpfu.ru/xmlui/handle/net/157754
dc.description.abstract © 2019 Elsevier Inc. Staphylococcus aureus hibernation promoting factor (SaHPF) is responsible for the formation of 100S ribosome dimers, which in turn help this pathogen to reduce energy spent under unfavorable conditions. Ribosome dimer formation strongly depends on the dimerization of the C-terminal domain of SaHPF (CTDSaHPF). In this study, we solved the crystal structure of CTDSaHPF at 1.6 Å resolution and obtained a precise arrangement of the dimer interface. Residues Phe160, Val162, Thr171, Ile173, Tyr175, Ile185 andThr187 in the dimer interface of SaHPF protein were mutated and the effects were analyzed for the formation of 100S disomes of ribosomes isolated from S. aureus. It was shown that substitution of any of single residues Phe160, Val162, Ile173, Tyr175 and Ile185 in the SaHPF homodimer interface abolished the ribosome dimerization in vitro.
dc.relation.ispartofseries Journal of Structural Biology
dc.subject Hibernation
dc.subject Long HPF
dc.subject Ribosome
dc.subject Staphylococcus aureus
dc.subject X-ray
dc.title Dimerization of long hibernation promoting factor from Staphylococcus aureus: Structural analysis and biochemical characterization
dc.type Article
dc.collection Публикации сотрудников КФУ
dc.source.id SCOPUS10478477-2019-SID85074516876


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  • Публикации сотрудников КФУ Scopus [24551]
    Коллекция содержит публикации сотрудников Казанского федерального (до 2010 года Казанского государственного) университета, проиндексированные в БД Scopus, начиная с 1970г.

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