Structure determination of uniformly C-13, N-15 labeled protein using qualitative distance restraints from MAS solid-state C-13-NMR observed paramagnetic relaxation enhancement

Tamaki, Hajime; Egawa, Ayako; Kido, Kouki; Kameda, Tomoshi; Kamiya, Masakatsu; Kikukawa, Takashi; Aizawa, Tomoyasu; Fujiwara, Toshimichi; Demura, Makoto

Structure determination of uniformly C-13, N-15 labeled protein using qualitative distance restraints from MAS solid-state C-13-NMR observed paramagnetic relaxation enhancement

Tamaki, Hajime; Egawa, Ayako; Kido, Kouki et al.

Journal of biomolecular NMR, 2016, 64(1), 87-101

Permalink : https://hdl.handle.net/2115/63937

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アクセス権	open access
URI	https://hdl.handle.net/2115/63937
タイトル	Structure determination of uniformly C-13, N-15 labeled protein using qualitative distance restraints from MAS solid-state C-13-NMR observed paramagnetic relaxation enhancement
著者	Tamaki, Hajime ; Egawa, Ayako ; Kido, Kouki ; Kameda, Tomoshi ; Kamiya, Masakatsu ; Kikukawa, Takashi ; Aizawa, Tomoyasu ; Fujiwara, Toshimichi ; Demura, Makoto
著者名 Tamaki, Hajime
著者名 Egawa, Ayako
著者名 Kido, Kouki
著者名 Kameda, Tomoshi
著者名 Kamiya, Masakatsu
著者名 Kikukawa, Takashi
著者名 Aizawa, Tomoyasu
著者名 Fujiwara, Toshimichi
著者名 Demura, Makoto
言語	英語
キーワード	Solid-state NMR
	Magic-angle spinning
	Protein structure
	Paramagnetic relaxation enhancement
	CS-Rosetta
発行日	2016-01
出版者	Springer
収録物名	Journal of biomolecular NMR
巻(号)	64(1)
ページ	87-101
抄録	Magic angle spinning (MAS) solid-state nuclear magnetic resonance (NMR) is a powerful method for structure determination of insoluble biomolecules. However, structure determination by MAS solid-state NMR remains challenging because it is difficult to obtain a sufficient amount of distance restraints owing to spectral complexity. Collection of distance restraints from paramagnetic relaxation enhancement (PRE) is a promising approach to alleviate this barrier. However, the precision of distance restraints provided by PRE is limited in solid-state NMR because of incomplete averaged interactions and intermolecular PREs. In this report, the backbone structure of the B1 domain of streptococcal protein G (GB1) has been successfully determined by combining the CS-Rosetta protocol and qualitative PRE restraints. The derived structure has a C alpha RMSD of 1.49 angstrom relative to the X-ray structure. It is noteworthy that our protocol can determine the correct structure from only three cysteine-EDTA-Mn2+ mutants because this number of PRE sites is insufficient when using a conventional structure calculation method based on restrained molecular dynamics and simulated annealing. This study shows that qualitative PRE restraints can be employed effectively for protein structure determination from a limited conformational sampling space using a protein fragment library.
資源タイプ	学術雑誌論文
出版タイプ	Accepted Manuscript
権利情報	The final publication is available at www.springerlink.com via http://dx.doi.org/10.1007/s10858-015-0010-0.
PISSN	0925-2738
関連情報	PMID 26728076
関連情報 (isVersionOf)	出版社版DOI https://doi.org/10.1007/s10858-015-0010-0