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J. Biol. Chem., Vol. 282, Issue 27, 19928-19937, July 6, 2007

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Human OLA1 Defines an ATPase Subfamily in the Obg Family of GTP-binding Proteins^*

Roland Koller-Eichhorn¹, Tobias Marquardt¹², Robert Gail^¶, Alfred Wittinghofer^¶, Dirk Kostrewa, Ulrike Kutay³, and Christian Kambach⁴

From the Institute of Biochemistry, ETH Zurich, 8093 Zurich, Switzerland, the Paul Scherrer Institute, Biomolecular Research, 5232 Villigen, Switzerland, and the ^¶Max-Planck-Institut für Molekulare Physiologie, Strukturelle Biologie, 44227 Dortmund, Germany

Purine nucleotide-binding proteins build the large family of P-loop GTPases and related ATPases, which perform essential functions in all kingdoms of life. The Obg family comprises a group of ancient GTPases belonging to the TRAFAC (for translation factors) class and can be subdivided into several distinct protein subfamilies. The founding member of one of these subfamilies is the bacterial P-loop NTPase YchF, which had so far been assumed to act as GTPase. We have biochemically characterized the human homologue of YchF and found that it binds and hydrolyzes ATP more efficiently than GTP. For this reason, we have termed the protein hOLA1, for human Obg-like ATPase 1. Further biochemical characterization of YchF proteins from different species revealed that ATPase activity is a general but previously missed feature of the YchF subfamily of Obg-like GTPases. To explain ATP specificity of hOLA1, we have solved the x-ray structure of hOLA1 bound to the nonhydrolyzable ATP analogue AMPPCP. Our structural data help to explain the altered nucleotide specificity of YchF homologues and identify the Ola1/YchF subfamily of the Obg-related NTPases as an exceptional example of a single protein subfamily, which has evolved altered nucleotide specificity within a distinct protein family of GTPases.

Received for publication, January 19, 1007 , and in revised form, April 4, 2007.

The atomic coordinates and structure factors (code 2OHF) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This work was supported by an intramural ETH grant (to R. K.-E. and U. K.) and by funding through the Swiss National Science Foundation (to U. K. and C. K.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Tables S1 and S2 and supplemental Figs. S1-S4.

¹ These authors contributed equally to this work.

² Present address: Bayer HealthCare AG, D-42096 Wuppertal, Germany.

³ To whom correspondence may be addressed: Institute of Biochemistry, HPM F11.1, Schafmattstr.18, ETH Zurich, 8093 Zurich, Switzerland. Tel.: 41-44-632-3013; Fax: 41-44-632-1591; E-mail: ulrike.kutay{at}bc.biol.ethz.ch.

⁴ To whom correspondence may be addressed: Paul Scherrer Institute, CH-5232 Villigen PSI, Switzerland. Tel.: 41-56-310-4723; Fax: 41-56-310-5288; E-mail: christian.kambach{at}psi.ch.

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