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J. Biol. Chem., Vol. 283, Issue 47, 32968-32976, November 21, 2008

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The Structure of YqeH

AN AtNOS1/AtNOA1 ORTHOLOG THAT COUPLES GTP HYDROLYSIS TO MOLECULAR RECOGNITION^*

Jawahar Sudhamsu, Gyu In Lee, Daniel F. Klessig, and Brian R. Crane¹

From the Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853 and Boyce Thompson Institute for Plant Research, Ithaca, New York 14853

AtNOS1/AtNOA1 was identified as a nitric oxide-generating enzyme in plants, but that function has recently been questioned. To resolve issues surrounding AtNOA1 activity, we report the biochemical properties and a 2.36 Å resolution crystal structure of a bacterial AtNOA1 ortholog (YqeH). Geobacillus YqeH fused to a putative AtNOA1 leader peptide complements growth and morphological defects of Atnoa1 mutant plants. YqeH does not synthesize nitric oxide from L-arginine but rather hydrolyzes GTP. The YqeH structure reveals a circularly permuted GTPase domain and an unusual C-terminal β-domain. A small N-terminal domain, disordered in the structure, binds zinc. Structural homology among the C-terminal domain, the RNA-binding regulator TRAP, and the hypoxia factor pVHL define a recognition module for peptides and nucleic acids. TRAP residues important for RNA binding are conserved by the YqeH C-terminal domain, whose positioning is coupled to GTP hydrolysis. YqeH and AtNOA1 probably act as G-proteins that regulate nucleic acid recognition and not as nitric-oxide synthases.

Received for publication, June 25, 2008 , and in revised form, September 8, 2008.

The atomic coordinates and structure factors (code 3EC1) 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, in whole or in part, by National Institutes of Health Grant 5R01GM067011 (to D. F. K.). This work was also supported by National Science Foundation Grant CHE-0749996 (to B. R. C.). 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 Table 1 and Figs. 1 and 2.

¹ To whom correspondence should be addressed: G60 S.T.OLIN, Cornell University, Ithaca, NY 14853. Tel.: 607-254-8634; Fax: 607-255-1248; E-mail: bc69{at}cornell.edu.

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