1VEE

NMR structure of the hypothetical rhodanese domain At4g01050 from Arabidopsis thaliana

1VEE の概要

• エントリーDOI: 10.2210/pdb1vee/pdb
• NMR情報: BMRB: 5929
• 分子名称: proline-rich protein family (1 entity in total)
• 機能のキーワード: hypothetical protein, structural genomics, rhodanese domain, riken structural genomics/proteomics initiative, rsgi, unknown function
• 由来する生物種: Arabidopsis thaliana (thale cress)
• 細胞内の位置: Plastid, chloroplast: Q9M158
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14201.86

構造登録者

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.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2004-03-30, 公開日: 2005-01-25, 最終更新日: 2023-12-27)

主引用文献

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.
Solution structure of the rhodanese homology domain At4g01050(175-295) from Arabidopsis thaliana
Protein Sci., 14:224-230, 2005

PubMed Abstract: 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.

PubMed: 15576557
DOI: 10.1110/ps.041138705

実験手法

SOLUTION NMR