HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 280, Issue 16, 16002-16008, April 22, 2005

This Article Full Text Full Text (PDF) All Versions of this Article: 280/16/16002    most recent M414541200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Kuratani, M. Articles by Yokoyama, S. Search for Related Content PubMed PubMed Citation Articles by Kuratani, M. Articles by Yokoyama, S. Social Bookmarking                      What's this?

Crystal Structure of tRNA Adenosine Deaminase (TadA) from Aquifex aeolicus^*

Mitsuo Kuratani, Ryohei Ishii, Yoshitaka Bessho¶, Ryuya Fukunaga, Toru Sengoku, Mikako Shirouzu¶, Shun-ichi Sekine¶, and Shigeyuki Yokoyama¶||

From the Department of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan, RIKEN Genomic Sciences Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan, and ^¶RIKEN Harima Institute at SPring-8, 1-1-1 Kouto, Mikazuki-cho, Sayo-gun, Hyogo 679-5148, Japan

The bacterial tRNA adenosine deaminase (TadA) generates inosine by deaminating the adenosine residue at the wobble position of tRNA^Arg-2. This modification is essential for the decoding system. In this study, we determined the crystal structure of Aquifex aeolicus TadA at a 1.8-Å resolution. This is the first structure of a deaminase acting on tRNA. A. aeolicus TadA has an // three-layered fold and forms a homodimer. The A. aeolicus TadA dimeric structure is completely different from the tetrameric structure of yeast CDD1, which deaminates mRNA and cytidine, but is similar to the dimeric structure of yeast cytosine deaminase. However, in the A. aeolicus TadA structure, the shapes of the C-terminal helix and the regions between the 4 and 5 strands are quite distinct from those of yeast cytosine deaminase and a large cavity is produced. This cavity contains many conserved amino acid residues that are likely to be involved in either catalysis or tRNA binding. We made a docking model of TadA with the tRNA anticodon stem loop.

Received for publication, December 27, 2004 , and in revised form, January 18, 2005.

^* This work was supported by a grant-in-aid for Scientific Research S from the Japan Society for Promotion of Science (JSPS), a grant-in-aid for Scientific Research in Priority Areas from the Ministry of Education, Culture, Sports, Science and Technology (MEXT) of Japan, the RIKEN Structural Genomics/Proteomics Initiative (RSGI), and the National Project on Protein Structural and Functional Analyses, MEXT. 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 atomic coordinates and structure factors (code 1WWR) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^|| To whom correspondence should be addressed. Tel.: 81-3-5841-4392; Fax: 81-3-5841-8057; E-mail: yokoyama{at}biochem.s.u-tokyo.ac.jp.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				M. A. T. Rubio, I. Pastar, K. W. Gaston, F. L. Ragone, C. J. Janzen, G. A. M. Cross, F. N. Papavasiliou, and J. D. Alfonzo An adenosine-to-inosine tRNA-editing enzyme that can perform C-to-U deamination of DNA PNAS, May 8, 2007; 104(19): 7821 - 7826. [Abstract] [Full Text] [PDF]

				H. Huthoff and M. H. Malim Identification of Amino Acid Residues in APOBEC3G Required for Regulation by Human Immunodeficiency Virus Type 1 Vif and Virion Encapsidation J. Virol., April 15, 2007; 81(8): 3807 - 3815. [Abstract] [Full Text] [PDF]

				S.-C. Chen, Y.-C. Chang, C.-H. Lin, C.-H. Lin, and S.-H. Liaw Crystal Structure of a Bifunctional Deaminase and Reductase from Bacillus subtilis Involved in Riboflavin Biosynthesis J. Biol. Chem., March 17, 2006; 281(11): 7605 - 7613. [Abstract] [Full Text] [PDF]

				M. R. Macbeth, H. L. Schubert, A. P. VanDemark, A. T. Lingam, C. P. Hill, and B. L. Bass Inositol Hexakisphosphate Is Bound in the ADAR2 Core and Required for RNA Editing Science, September 2, 2005; 309(5740): 1534 - 1539. [Abstract] [Full Text] [PDF]