This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Kostelecky, B. Articles by Meyer-Klaucke, W. Search for Related Content PubMed PubMed Citation Articles by Kostelecky, B. Articles by Meyer-Klaucke, W.

 Previous Article  |  Next Article 

Journal of Bacteriology, February 2006, p. 1607-1614, Vol. 188, No. 4
0021-9193/06/$08.00+0     doi:10.1128/JB.188.4.1607-1614.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

The Crystal Structure of the Zinc Phosphodiesterase from Escherichia coli Provides Insight into Function and Cooperativity of tRNase Z-Family Proteins

Brenda Kostelecky,^1, Ehmke Pohl,² Andreas Vogel,^1, Oliver Schilling,^1, and Wolfram Meyer-Klaucke^1*

EMBL Hamburg Outstation, c/o DESY, Notkestrasse 85, D-22603 Hamburg, Germany,¹ Paul Scherrer Institut, CH-5232 Villigen PSI, Switzerland²

Received 3 August 2005/ Accepted 28 November 2005

The elaC gene product from Escherichia coli, ZiPD, is a 3' tRNA-processing endonuclease belonging to the tRNase Z family of enzymes that have been identified in a wide variety of organisms. In contrast to the elaC homologue from Bacillus subtilis, E. coli elaC is not essential for viability, and although both enzymes process only precursor tRNA (pre-tRNA) lacking a CCA triplet at the 3' end in vitro, the physiological role of ZiPD remains enigmatic because all pre-tRNA species in E. coli are transcribed with the CCA triplet. We present the first crystal structure of ZiPD determined by multiple anomalous diffraction at a resolution of 2.9 Å. This structure shares many features with the tRNase Z enzymes from B. subtilis and Thermotoga maritima, but there are distinct differences in metal binding and overall domain organization. Unlike the previously described homologous structures, ZiPD dimers display crystallographic symmetry and fully loaded metal sites. The ZiPD exosite is similar to that of the B. subtilis enzyme structurally, but its position with respect to the protein core differs substantially, illustrating its ability to act as a clamp in binding tRNA. Furthermore, the ZiPD crystal structure presented here provides insight into the enzyme's cooperativity and assists the ongoing attempt to elucidate the physiological function of this protein.

Present address: Cancer Research UK, 44 Lincoln's Inn Fields, London WC2A 3PX, United Kingdom.

Present address: Max-Planck-Institut für Kohlenforschung, Kaiser-Wilhelm-Platz 1, D-45470 Mülheim/Ruhr, Germany.

Present address: Department of Oral Biological & Medical Sciences, University of British Columbia, Vancouver, Canada.

This article has been cited by other articles:

• Minagawa, A., Takaku, H., Ishii, R., Takagi, M., Yokoyama, S., Nashimoto, M. (2006). Identification by Mn2+ rescue of two residues essential for the proton transfer of tRNase Z catalysis. Nucleic Acids Res 34: 3811-3818 [Abstract] [Full Text]  
• Zareen, N., Hopkinson, A., Levinger, L. (2006). Residues in two homology blocks on the amino side of the tRNase Z His domain contribute unexpectedly to pre-tRNA 3' end processing. RNA 12: 1104-1115 [Abstract] [Full Text]