Structure Note

Solution NMR structure of the ribosomal protein RP-L35Ae from Pyrococcus furiosus†

  1. David A. Snyder1,2,
  2. James M. Aramini2,
  3. Bomina Yu2,
  4. Yuanpeng J. Huang2,
  5. Rong Xiao2,
  6. John R. Cort3,
  7. Ritu Shastry2,
  8. Li-Chung Ma2,
  9. Jinfeng Liu4,
  10. Burkhard Rost4,
  11. Thomas B. Acton2,
  12. Michael A. Kennedy5,
  13. Gaetano T. Montelione2,6,*

Article first published online: 16 APR 2012

DOI: 10.1002/prot.24071

Issue

Proteins: Structure, Function, and Bioinformatics

Proteins: Structure, Function, and Bioinformatics

Volume 80, Issue 7, pages 1901–1906, July 2012

Additional Information

How to Cite

Snyder, D. A., Aramini, J. M., Yu, B., Huang, Y. J., Xiao, R., Cort, J. R., Shastry, R., Ma, L.-C., Liu, J., Rost, B., Acton, T. B., Kennedy, M. A. and Montelione, G. T. (2012), Solution NMR structure of the ribosomal protein RP-L35Ae from Pyrococcus furiosus. Proteins, 80: 1901–1906. doi: 10.1002/prot.24071

Author Information

  1. 1

    Department of Chemistry, College of Science and Health, William Paterson University, Wayne, New Jersey 07470

  2. 2

    Department of Molecular Biology and Biochemistry, Center for Advanced Biotechnology and Medicine, and The Northeast Structural Genomics Consortium, Rutgers, The State University of New Jersey, Piscataway, New Jersey 08854

  3. 3

    Biological Sciences Division, Pacific Northwest National Laboratory, and The Northeast Structural Genomics Consortium, Richland, Washington 99352

  4. 4

    Department of Biochemistry and Molecular Biophysics, Center for Computational Biology and Bioinformatics, andThe Northeast Structural Genomics Consortium, Columbia University, New York, New York 10032

  5. 5

    Department of Chemistry and Biochemistry, and The Northeast Structural Genomics Consortium, Miami University, Oxford, Ohio 45056

  6. 6

    Department of Biochemistry, Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey, Piscataway, New Jersey 08854

*CABM, Rutgers University, 679 Hoes Lane, Piscataway, NJ 08854

  1. †

    Partial support was also provided to David A. Snyder as Assigned Release Time from William Paterson University

Publication History

  1. Issue published online: 5 JUN 2012
  2. Article first published online: 16 APR 2012
  3. Accepted manuscript online: 16 MAR 2012 03:48AM EST
  4. Manuscript Accepted: 3 MAR 2012
  5. Manuscript Received: 7 FEB 2012

Funded by

  • National Institute of General Medical Sciences Protein Structure Initiative (PSI). Grant Numbers: U54-GM074958, U54-GM094597

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Keywords:

  • ribosomal protein;
  • L35Ae;
  • PF01247;
  • tRNA binding;
  • EF-Tu/eEF-1A;
  • solution NMR;
  • structural genomics

Abstract

The ribosome consists of small and large subunits each composed of dozens of proteins and RNA molecules. However, the functions of many of the individual protomers within the ribosome are still unknown. In this article, we describe the solution NMR structure of the ribosomal protein RP-L35Ae from the archaeon Pyrococcus furiosus. RP-L35Ae is buried within the large subunit of the ribosome and belongs to Pfam protein domain family PF01247, which is highly conserved in eukaryotes, present in a few archaeal genomes, but absent in bacteria. The protein adopts a six-stranded anti-parallel β-barrel analogous to the “tRNA binding motif” fold. The structure of the P. furiosus RP-L35Ae presented in this article constitutes the first structural representative from this protein domain family. Proteins 2012. © 2012 Wiley Periodicals, Inc.

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