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The structure of Rph, an exoribonuclease from Bacillus anthracis, at 1.7 angstrom resolution

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JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
DatePublished - Jan 2009
Issue numberPart 1
Volume65
Number of pages5
Pages (from-to)2-7
Original languageEnglish

Abstract

Maturation of tRNA precursors into functional tRNA molecules requires trimming of the primary transcript at both the 5' and 3' ends. Cleavage of nucleotides from the 3' stem of tRNA precursors, releasing nucleotide diphosphates, is accomplished in Bacillus by a phosphate-dependent exoribonuclease, Rph. The crystal structure of this enzyme from B. anthracis has been solved by molecular replacement to a resolution of 1.7 angstrom and refined to an R factor of 19.3%. There is one molecule in the asymmetric unit; the crystal packing reveals the assembly of the protein into a hexamer arranged as a trimer of dimers. The structure shows two sulfate ions bound in the active-site pocket, probably mimicking the phosphate substrate and the phosphate of the 3'-terminal nucleotide of the tRNA precursor. Three other bound sulfate ions point to likely RNA-binding sites.

Bibliographical note

© 2009 International Union of Crystallography. This is an author produced version of a paper published in ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS. Uploaded in accordance with the publisher's self archiving policy.

    Research areas

  • TRANSFER-RNA PRECURSORS, RAY-DIFFRACTION DATA, CRYSTAL-STRUCTURE, POLYNUCLEOTIDE PHOSPHORYLASE, PH, SUBTILIS, SEQUENCE, CRYSTALLIZATION, CLONING

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