КФУ. Карточка публикации. NMR assignments and secondary structure determination of the N-terminal domain of Ribosome maturation factor M from of Staphylococcus aureus

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NMR ASSIGNMENTS AND SECONDARY STRUCTURE DETERMINATION OF THE N-TERMINAL DOMAIN OF RIBOSOME MATURATION FACTOR M FROM OF STAPHYLOCOCCUS AUREUS

Форма представления

Статьи в российских журналах и сборниках

Год публикации

2021

Язык

английский

Авторы, сотрудники КФУ

Бикмуллин Айдар Галимзанович, автор

Валидов Шамиль Завдатович, автор

Клочков Владимир Васильевич, автор

Клочкова Эвелина Андреевна, автор

Кучаев Евгений Сергеевич, автор

Усачев Константин Сергеевич, автор

Юсупов Марат Миратович, автор

Авторы, аспиранты КФУ

Гараева Наталия Сергеевна, автор

Библиографическое описание на языке оригинала

Garaeva N.S., NMR assignments and secondary structure determination of the N-terminal domain of Ribosome maturation factor M from of Staphylococcus aureus / N.S. Garaeva, A.G. Bikmullin, E.S. Kuchaev, E.A. Klochkova, Sh.Z. Validov, V.V. Klochkov, A.V. Aganov, M.M. Yusupov, K.S. Usachev // Russian Chemical Bulletin. – 2021. – V. 12. – P. 2440-2444.

Аннотация

The ribosome maturation factor M (RimM) is a protein with a molecular mass of 19.072 kDa involved in assembling of the 30S ribosome subunit. The RimM is necessary for the efficient processing of 16S rRNA. However, the mechanism of interaction of the RimM N-terminal domain with 16S rRNA remains poorly studied. The synthesis of the N-terminal domain of RimM from Staphylococcus aureus enriched in 13C and 15N isotopes and subsequent analysis of chemical shifts of the 1H, 13C, and 15N signals from the backbone and side chains are described. An analysis of chemical shifts suggests that the N-terminal domain of RimM contains six β-chains and three α-helices with the topology β1-β2-α1-β3-β4-β5-α2-β6-β3. The secondary structure of the N-terminal domain of RimM contains a KH domain between the β1 and β2 fold with a strongly conserved segment with the GXXG sequence. The further structural studies by integrated structural biology approach (NMR spectroscopy, X-ray diffraction analysis, and cryoelectron microscopy) of RimM and its complex with ribosome will allow screening of highly selective inhibitors of Staphylococcus aureus translation.

Ключевые слова

NMR, Staphylococcus aureus

Название журнала

Russian Chemical Bulletin

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https://repository.kpfu.ru/?p_id=264779

Полная запись метаданных

Поле DC	Значение	Язык
dc.contributor.author	Бикмуллин Айдар Галимзанович	ru_RU
dc.contributor.author	Валидов Шамиль Завдатович	ru_RU
dc.contributor.author	Клочков Владимир Васильевич	ru_RU
dc.contributor.author	Клочкова Эвелина Андреевна	ru_RU
dc.contributor.author	Кучаев Евгений Сергеевич	ru_RU
dc.contributor.author	Усачев Константин Сергеевич	ru_RU
dc.contributor.author	Юсупов Марат Миратович	ru_RU
dc.contributor.author	Гараева Наталия Сергеевна	ru_RU
dc.date.accessioned	2021-01-01T00:00:00Z	ru_RU
dc.date.available	2021-01-01T00:00:00Z	ru_RU
dc.date.issued	2021	ru_RU
dc.identifier.citation	Garaeva N.S., NMR assignments and secondary structure determination of the N-terminal domain of Ribosome maturation factor M from of Staphylococcus aureus / N.S. Garaeva, A.G. Bikmullin, E.S. Kuchaev, E.A. Klochkova, Sh.Z. Validov, V.V. Klochkov, A.V. Aganov, M.M. Yusupov, K.S. Usachev // Russian Chemical Bulletin. – 2021. – V. 12. – P. 2440-2444.	ru_RU
dc.identifier.uri	https://repository.kpfu.ru/?p_id=264779	ru_RU
dc.description.abstract	Russian Chemical Bulletin	ru_RU
dc.description.abstract	The ribosome maturation factor M (RimM) is a protein with a molecular mass of 19.072 kDa involved in assembling of the 30S ribosome subunit. The RimM is necessary for the efficient processing of 16S rRNA. However, the mechanism of interaction of the RimM N-terminal domain with 16S rRNA remains poorly studied. The synthesis of the N-terminal domain of RimM from Staphylococcus aureus enriched in 13C and 15N isotopes and subsequent analysis of chemical shifts of the 1H, 13C, and 15N signals from the backbone and side chains are described. An analysis of chemical shifts suggests that the N-terminal domain of RimM contains six β-chains and three α-helices with the topology β1-β2-α1-β3-β4-β5-α2-β6-β3. The secondary structure of the N-terminal domain of RimM contains a KH domain between the β1 and β2 fold with a strongly conserved segment with the GXXG sequence. The further structural studies by integrated structural biology approach (NMR spectroscopy, X-ray diffraction analysis, and cryoelectron microscopy) of RimM and its complex with ribosome will allow screening of highly selective inhibitors of Staphylococcus aureus translation.	ru_RU
dc.language.iso	ru	ru_RU
dc.subject	NMR	ru_RU
dc.subject	Staphylococcus aureus	ru_RU
dc.title	NMR assignments and secondary structure determination of the N-terminal domain of Ribosome maturation factor M from of Staphylococcus aureus	ru_RU
dc.type	Статьи в российских журналах и сборниках	ru_RU