Journal
JOURNAL OF BIOMOLECULAR NMR
Volume 61, Issue 1, Pages 55-64Publisher
SPRINGER
DOI: 10.1007/s10858-014-9882-7
Keywords
Paramagnetic relaxation enhancement; PRE; Structure determination; Soluble protein; RDC; Sin1
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Funding
- MEXT/JSPS KAKENHI
- TPRP
- Platform for Drug Discovery, Informatics, and Structural Life Science
- Grants-in-Aid for Scientific Research [26291013, 26291024, 26650018] Funding Source: KAKEN
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NMR structure determination of soluble proteins depends in large part on distance restraints derived from NOE. In this study, we examined the impact of paramagnetic relaxation enhancement (PRE)-derived distance restraints on protein structure determination. A high-resolution structure of the loop-rich soluble protein Sin1 could not be determined by conventional NOE-based procedures due to an insufficient number of NOE restraints. By using the 867 PRE-derived distance restraints obtained from the NOE-based structure determination procedure, a high-resolution structure of Sin1 could be successfully determined. The convergence and accuracy of the determined structure were improved by increasing the number of PRE-derived distance restraints. This study demonstrates that PRE-derived distance restraints are useful in the determination of a high-resolution structure of a soluble protein when the number of NOE constraints is insufficient.
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