Dynamics of backbone conformational heterogeneity in Bacillus subtilis ribonuclease P protein

Christopher H. Henkels, Yu Chu Chang, Stacy I. Chamberlin, Terrence G. Oas

研究成果: 雜誌貢獻文章同行評審

4 引文 斯高帕斯(Scopus)

摘要

Interconversion of protein conformations is imperative to function, as evidenced by conformational changes associated with enzyme catalytic cycles, ligand binding and post-translational modifications. In this study, we used 15N NMR relaxation experiments to probe the fast (i.e., ps-ns) and slow (i.e., μs-ms) conformational dynamics of Bacillus subtilis ribonuclease P protein (P protein) in its folded state, bound to two sulfate anions. Using the Lipari-Szabo mapping method [Andrec, M., Montelione, G. T., and Levy, R. M. (2000) J. Biomol. NMR 18, 83-100] to interpret the data, we find evidence for P protein dynamics on the μs-ms time scale in the ensemble. The residues that exhibit these slow internal motions are found in regions that have been previously identified as part of the P protein-P RNA interface. These results suggest that structural flexibility within the P protein ensemble may be important for proper RNase P holoenzyme assembly and/or catalysis.
原文英語
頁(從 - 到)15062-15075
頁數14
期刊Biochemistry
46
發行號51
DOIs
出版狀態已發佈 - 12月 25 2007
對外發佈

ASJC Scopus subject areas

  • 生物化學

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