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Protein Science (2005), 14:719-726. Published by Cold Spring Harbor Laboratory Press. Copyright © 2005 The Protein Society
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Structure and mechanism of ADP-ribose-1''-monophosphatase (Appr-1''-pase), a ubiquitous cellular processing enzyme

Desigan Kumaran, Subramaniam Eswaramoorthy, F. William Studier and Subramanyam Swaminathan

Biology Department, Brookhaven National Laboratory, Upton, New York 11973, USA

(RECEIVED September 18, 2004; FINAL REVISION November 25, 2004; ACCEPTED November 29, 2004)

Appr-1''-pase, an important and ubiquitous cellular processing enzyme involved in the tRNA splicing pathway, catalyzes the conversion of ADP-ribose-1''monophosphate (Appr-1''-p) to ADP-ribose. The structures of the native enzyme from the yeast and its complex with ADP-ribose were determined to 1.9 Å and 2.05 Å, respectively. Analysis of the three-dimensional structure of this protein, selected as a target in a structural genomics project, reveals its putative function and provides clues to the catalytic mechanism. The structure of the 284-amino acid protein shows a two-domain architecture consisting of a three-layer {alpha}{beta}{alpha} sandwich N-terminal domain connected to a small C-terminal helical domain. The structure of Appr-1''-pase in complex with the product, ADP-ribose, reveals an active-site water molecule poised for nucleophilic attack on the terminal phosphate group. Loop-region residues Asn 80, Asp 90, and His 145 may form a catalytic triad.

Keywords: ADP-ribose-1''-monophosphate; tRNA splicing pathway; structural genomics; X-ray structure

Article and publication are at http://www.proteinscience.org/cgi/doi/10.1110/ps.041132005.

Reprint requests to: Subramanyam Swaminathan, Biology Department, Brookhaven National Laboratory, Upton, NY 11973, USA; e-mail: swami{at}bnl.gov; fax: (631) 344-3407.


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