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1 Tatsuo Miyazawa Memorial Program, 2 RIKEN Genomic Sciences Center, 1-7-22, Suehiro, Tsurumi, Yokohama 230-0045, Japan
3 RIKEN Harima Institute at Spring-8, 1-1-1 Kouto, Mikazuki, Sayo, Hyogo 679-5148, Japan
4 Department of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo, Tokyo 113-0033, Japan
(RECEIVED September 23, 2004; FINAL REVISION September 25, 2004; ACCEPTED September 27, 2004)
The three-dimensional structure of the rhodanese homology domain At4g01050(175195) from Arabidopsis thaliana has been determined by solution nuclear magnetic resonance methods based on 3043 upper distance limits derived from NOE intensities measured in three-dimensional NOESY spectra. The structure shows a backbone root mean square deviation to the mean coordinates of 0.43 Å for the structured residues 7125. The fold consists of a central parallel
-sheet with five strands in the order 15423 and arranged in the conventional counterclockwise twist, and helices packing against each side of the
-sheet. Comparison with the sequences of other proteins with a rhodanese homology domain in Arabidopsis thaliana indicated residues that could play an important role in the scaffold of the rhodanese homology domain. Finally, a three-dimensional structure comparison of the present noncatalytic rhodanese homology domain with the noncatalytic rhodanese domains of sulfurtransferases from other organisms discloses differences in the length and conformation of loops that could throw light on the role of the noncatalytic rhodanese domain in sulfurtransferases.
Keywords: structural genomics; protein structure; rhodanese; At4g01050; high-throughput NMR; Arabidopsis thaliana
Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.041138705.
Reprint requests to: Peter Güntert, RIKEN Genomic Sciences Center, 1-7-22, Suehiro, Tsurumi, Yokohama 230-0045, Japan; e-mail: guentert{at}gsc.riken.jp; fax: +81-45-503-9343.
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