1TH5

Solution structure of C-terminal domain of NifU-like protein from Oryza sativa

1TH5 の概要

• エントリーDOI: 10.2210/pdb1th5/pdb
• 関連するPDBエントリー: 1Q48
• NMR情報: BMRB: 6247
• 分子名称: NifU1 (1 entity in total)
• 機能のキーワード: iron-sulfur cluster binding, structural genomics, program for rice genome research, unknown function
• 由来する生物種: Oryza sativa (rice)
• 細胞内の位置: Plastid, chloroplast stroma (By similarity): Q84LK7
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8105.71

構造登録者

Kumeta, H.,Ogura, K.,Asayama, M.,Katoh, S.,Katoh, E.,Inagaki, F. (登録日: 2004-06-01, 公開日: 2005-09-27, 最終更新日: 2024-05-29)

主引用文献

Kumeta, H.,Ogura, K.,Asayama, M.,Katoh, S.,Katoh, E.,Teshima, K.,Inagaki, F.
The NMR structure of the domain II of a chloroplastic NifU-like protein OsNifU1A.
J.Biomol.Nmr, 38:161-164, 2007

PubMed Abstract: NifU-like proteins are a highly conserved protein that serves as the scaffold for assembly of Fe-S clusters. Chloroplastic NifU-like proteins have tandem NifU like domains, named domain I and domain II. Although the amino acid sequences of these domains are very similar to each other, the predicted functional region for the Fe-S cluster assembly, the CXXC motif, exists only in domain I. The structure of the domain II of chloroplastic NifU-like protein OsNifU1A has an alpha-beta sandwich structure containing two alpha helices located on one side of the beta-sheet. The electrostatic surface potential of OsNifU1A domain II is predominantly positively charged. Chloroplastic NifU-like proteins are targeted to ferredoxin for transferring the Fe-S cluster. The ferredoxin presents an overall negatively charged surface, which may evoke an electrostatic association with OsNifU1A domain II.

PubMed: 17431550
DOI: 10.1007/s10858-007-9155-9

実験手法

SOLUTION NMR