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Inherent protein structural flexibility at the RNA-binding interface of L30e

Academic Article
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Overview

related to degree

  • Chao, Jeffrey Alan, Ph.D. in Macromolecular and Cellular Structure and Chemistry, Scripps Research 1999 - 2005

authors

  • Chao, Jeffrey Alan
  • Prasad, G. S.
  • White, S. A.
  • Stout, C. David
  • Williamson, James

publication date

  • February 2003

journal

  • Journal of Molecular Biology  Journal

abstract

  • The Saccharomyces cerevisiae ribosomal protein L30 autoregulates its own expression by binding to a purine-rich internal loop in its pre-mRNA and mRNA. NMR studies of L30 and its RNA complex showed that both the internal loop of the RNA as well as a region of the protein become substantially more ordered upon binding. A crystal structure of a maltose binding protein (MBP)-L30 fusion protein with two copies in the asymmetric unit has been determined. The flexible RNA-binding region in the L30 copies has two distinct conformations, one resembles the RNA bound form solved by NMR and the other is unique. Structure prediction algorithms also had difficulty accurately predicting this region, which is consistent with conformational flexibility seen in the NMR and X-ray crystallography studies. Inherent conformational flexibility may be a hallmark of regions involved in intermolecular interactions.

subject areas

  • Amino Acid Sequence
  • Binding Sites
  • Crystallography, X-Ray
  • Models, Molecular
  • Molecular Sequence Data
  • Nucleic Acid Conformation
  • Protein Structure, Tertiary
  • RNA
  • RNA-Binding Proteins
  • Ribosomal Proteins
  • Saccharomyces cerevisiae Proteins
  • Sequence Alignment
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Research

keywords

  • MBP-L30 fusion protein
  • autoregulation
  • induced fit
  • protein structural flexibility
  • ribosomal protein L30
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Identity

International Standard Serial Number (ISSN)

  • 0022-2836

Digital Object Identifier (DOI)

  • 10.1016/s0022-2836(02)01476-6

PubMed ID

  • 12589748
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Additional Document Info

start page

  • 999

end page

  • 1004

volume

  • 326

issue

  • 4

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