KFU. Card publication. 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

Form of presentation

Articles in Russian journals and collections

Year of publication

2021

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Authors, employees of KFU

Bikmullin Aydar Galimzanovich, author

Validov Shamil Zavdatovich, author

Klochkov Vladimir Vasilevich, author

Klochkova Evelina Andreevna, author

Kuchaev Evgeniy Sergeevich, author

Usachev Konstantin Sergeevich, author

Yusupov Marat Miratovich, author

Authors, postgraduates KFU

Garaeva Nataliya Sergeevna, postgraduate kfu

Bibliographic description in the original language

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.

Annotation

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.

Keywords

NMR, Staphylococcus aureus

The name of the journal

Russian Chemical Bulletin

Please use this ID to quote from or refer to the card

https://repository.kpfu.ru/eng/?p_id=264779&p_lang=2

Full metadata record

Field DC	Value	Language
dc.contributor.author	Bikmullin Aydar Galimzanovich	ru_RU
dc.contributor.author	Validov Shamil Zavdatovich	ru_RU
dc.contributor.author	Klochkov Vladimir Vasilevich	ru_RU
dc.contributor.author	Klochkova Evelina Andreevna	ru_RU
dc.contributor.author	Kuchaev Evgeniy Sergeevich	ru_RU
dc.contributor.author	Usachev Konstantin Sergeevich	ru_RU
dc.contributor.author	Yusupov Marat Miratovich	ru_RU
dc.contributor.author	Garaeva Nataliya Sergeevna	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/eng/?p_id=264779&p_lang=2	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	Articles in Russian journals and collections	ru_RU