Analysis of internal motions of RNase T1 complexed with a productive substrate involving 15N NMR relaxation measurements

Yuichiro Yoshida, Masakazu Tanaka, Takatoshi Ohkuri, Yoshitsugu Tanaka, Taiji Imoto, Tadashi Ueda

Research output: Contribution to journalArticle

Abstract

The backbone dynamics of RNase T1 in the presence of exo-guanosine 2′,3′-cyclophosphorothioate (exo-cGPS isomer), which is a productive substrate, and in the presence of 3′-guanylic acid (3′GMP), which is an nonproductive substrate, were examined using 15N nuclear magnetic resonance. Although the X-ray crystal structure suggests that the modes of binding of these substrates to the active-site cleft are very similar, the order parameters in a number of regions in RNase T1 complexed with exo-cGPS isomer were different from those with 3′GMP. Moreover, the chemical exchange in line width observed for RNase T1 complexed with exo-cGPS isomer was also different from that observed for RNase T1 complexed with 3′GMP. From these results, we concluded that the internal motions in RNase T1 complexed with a productive substrate were not always identical to those in RNase T1 complexed with a nonproductive substrate.

Original languageEnglish
Pages (from-to)43-48
Number of pages6
JournalJournal of biochemistry
Volume140
Issue number1
DOIs
Publication statusPublished - Jul 1 2006

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

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