1vee

File:1vee.gif

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NMR structure of the hypothetical rhodanese domain At4g01050 from Arabidopsis thaliana

OverviewOverview

The three-dimensional structure of the rhodanese homology domain, At4g01050(175-195) 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 A for the structured residues 7-125. The fold, consists of a central parallel beta-sheet with five strands in the order, 1-5-4-2-3 and arranged in the conventional counterclockwise twist, and, helices packing against each side of the beta-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.

About this StructureAbout this Structure

1VEE is a Single protein structure of sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.

ReferenceReference

Solution structure of the rhodanese homology domain At4g01050(175-295) from Arabidopsis thaliana., Pantoja-Uceda D, Lopez-Mendez B, Koshiba S, Inoue M, Kigawa T, Terada T, Shirouzu M, Tanaka A, Seki M, Shinozaki K, Yokoyama S, Guntert P, Protein Sci. 2005 Jan;14(1):224-30. Epub 2004 Dec 2. PMID:15576557

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