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

Rawlings, Andrea E., Blagova, Elena V., Levdikov, Vladimir M., Fogg, Mark J., Wilson, Keith S. (orcid.org/0000-0002-3581-2194) and Wilkinson, Anthony J. (orcid.org/0000-0003-4577-9479) (2009) The structure of Rph, an exoribonuclease from Bacillus anthracis, at 1.7 angstrom resolution. Acta Crystallographica Section F: Structural Biology and Crystallization Communications. pp. 2-7. ISSN 1744-3091

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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.

Item Type: Article
Copyright, Publisher and Additional Information: © 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.
Institution: The University of York
Academic Units: The University of York > Chemistry (York)
Depositing User: Repository Administrator York
Date Deposited: 06 Feb 2009 14:57
Last Modified: 22 Mar 2016 00:02
Published Version: http://dx.doi.org/10.1107/S1744309108041511
Status: Published
Refereed: Yes
Related URLs:
URI: http://eprints.whiterose.ac.uk/id/eprint/7653

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