NMR resonance assignments of the archaeal ribosomal protein L7Ae in the apo form and bound to a 25 nt RNA

详细信息    查看全文

• 作者：Thomas Moschen ; Christoph Wunderlich ; Christoph Kreutz…
• 关键词：NMR ; Assignment ; L7Ae ; Kink ; turn ; Ribosomal protein
• 刊名：Biomolecular NMR Assignments
• 出版年：2015
• 出版时间：April 2015
• 年：2015
• 卷：9
• 期：1
• 页码：177-180
• 全文大小：1,112 KB
• 参考文献：1. Delaglio, F, Grzesiek, S, Vuister, GW, Zhu, G, Pfeifer, J, Bax, A (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6: pp. 227-293 CrossRef
  2. Hamma, T, Ferré-D’Amaré, AR (2004) Structure of protein L7Ae bound to a K-turn derived from an archaeal box H/ACA sRNA at 1.8 A resolution. Structure 12: pp. 893-903 CrossRef
  3. Huang, L, Lilley, DMJ (2013) The molecular recognition of kink-turn structure by the L7Ae class of proteins. RNA 19: pp. 1703-1710 CrossRef
  4. Korzhnev, DM, Religa, TL, Kay, LE (2012) Transiently populated intermediate functions as a branching point of the FF domain folding pathway. Proc Natl Acad Sci USA 109: pp. 17777-17782 CrossRef
  5. Shen, Y, Delaglio, F, Cornilescu, G, Bax, A (2009) TALOS+ : a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. J Biomol NMR 44: pp. 213-223 CrossRef
  6. Suryadi, J, Tran, EJ, Maxwell, ES, Brown, BA (2005) The crystal structure of the Methanocaldococcus jannaschii multifunctional L7Ae RNA-binding protein reveals an induced-fit interaction with the box C/D RNAs. Biochemistry 44: pp. 9657-9672 CrossRef
  7. Tamiola, K, Burcin, A, Mulder, FAA (2010) Sequence-specific random coil chemical shifts of intrinsically disordered proteins. J Am Chem Soc 132: pp. 18000-18003 CrossRef
  8. Vranken, WF, Boucher, W, Stevens, TJ, Fogh, RH, Pajon, A, Llinas, M, Ulrich, EL, Markley, JL, Ionides, J, Laue, ED (2005) The CCPN data model for NMR spectroscopy: development of a software pipeline. Proteins 59: pp. 687-696 CrossRef
  
• 刊物类别：Physics and Astronomy
• 刊物主题：None Assigned
• 出版者：Springer Netherlands
• ISSN：1874-270X

文摘

The archaeal protein L7Ae forms part of a protein complex in the ribosome that specifically recognizes and binds to kink-turn RNA. In this complex, L7Ae directly interacts with the oligonucleotide and creates a functional arrangement for site-specific 2-O-methylation. We report the solution NMR backbone assignment of Methanocaldococcus jannaschii L7Ae (117 residues, 12.7?kDa) in the ligand-free state and when bound to a 25 nucleotide C/D box kink-turn mimic RNA.