The 1.2 Å crystal structure of an E. coli tRNASer acceptor stem microhelix reveals two magnesium binding sites

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Erscheinungsjahr:
2009
Medientyp:
Text
Schlagworte:
  • Amino Acyl-tRNA Synthetases
  • RNA
  • Transfer
  • Genetic code
  • Ribosomes
  • Proteins
  • tRNA acceptor stem microhelix
  • Magnesium binding sites
  • Identity elements
  • RNA hydration
  • tRNASer/Seryl-tRNA-synthetase
  • X-ray structure
  • Amino Acyl-tRNA Synthetases
  • RNA
  • Transfer
  • Genetic code
  • Ribosomes
  • Proteins
Beschreibung:
  • tRNA identity elements assure the correct aminoacylation of tRNAs by the cognate aminoacyl-tRNA synthetases. tRNASer belongs to the so-called class II system, in which the identity elements are rather simple and are mostly located in the acceptor stem region, in contrast to 'class I', where tRNA determinants are more complex and are located within different regions of the tRNA. The structure of an Escherichia coli tRNASer acceptor stem microhelix was solved by high resolution X-ray structure analysis. The RNA crystallizes in the space group C2, with one molecule per asymmetric unit and with the cell constants a = 35.79, b = 39.13, c = 31.37 Å, and β = 111.1°. A defined hydration pattern of 97 water molecules surrounds the tRNASer acceptor stem microhelix. Additionally, two magnesium binding sites were detected in the tRNASer aminoacyl stem. © 2009 Elsevier Inc. All rights reserved.
Lizenz:
  • info:eu-repo/semantics/closedAccess
Quellsystem:
Forschungsinformationssystem der UHH
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oai:www.edit.fis.uni-hamburg.de:publications/f82d8bf0-dd94-4250-95a2-8212aebb942e