Utilization of paramagnetic relaxation enhancements for high-resolution NMR structure determination of a soluble loop-rich protein with sparse NOE distance restraints

Kyoko Furuita, Saori Kataoka, Toshihiko Sugiki, Yoshikazu Hattori, Naohiro Kobayashi, Takahisa Ikegami, Kazuhiro Shiozaki, Toshimichi Fujiwara, Chojiro Kojima

Research output: Contribution to journalArticle

10 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)55-64
Number of pages10
JournalJournal of Biomolecular NMR
Volume61
Issue number1
DOIs
StatePublished - 2015
Externally publishedYes

Keywords

  • Paramagnetic relaxation enhancement
  • PRE
  • RDC
  • Sin1
  • Soluble protein
  • Structure determination

ASJC Scopus subject areas

  • Spectroscopy
  • Biochemistry

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