2JNV

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

2JNV の概要

• エントリーDOI: 10.2210/pdb2jnv/pdb
• 関連するPDBエントリー: 1TH5 1VEH
• 分子名称: NifU-like protein 1, chloroplast (1 entity in total)
• 機能のキーワード: iron-sulfur cluster binding, program for rice genome reserch, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, metal transport
• 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: 9823.24

構造登録者

Saio, T.,Ogura, K.,Kumeta, H.,Yokochi, M.,Katoh, S.,Katoh, E.,Inagaki, F.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2007-02-06, 公開日: 2007-12-18, 最終更新日: 2023-12-20)

主引用文献

Saio, T.,Kumeta, H.,Ogura, K.,Yokochi, M.,Asayama, M.,Katoh, S.,Katoh, E.,Teshima, K.,Inagaki, F.
The cooperative role of OsCnfU-1A domain I and domain II in the iron sulphur cluster transfer process as revealed by NMR
J.Biochem.(Tokyo), 142:113-121, 2007

PubMed Abstract: OsCnfU-1A is a chloroplast-type Nfu-like protein that consists of tandem repeats sharing high sequence homology. Domain I of this protein, but not domain II, has a C-X-X-C motif that is thought to assemble an iron-sulphur cluster. Herein we report the solution structure of OsCnfU-1A domain I (73-153). Although OsCnfU-1A domain I is structurally similar to OsCnfU-1A domain II (154-226), the electrostatic surface potential of the 2 domains differs. Domain I has an acidic surface, whereas that of domain II is predominantly basic. Chemical shift perturbation studies on OsCnfU-1A domain I and domain II with ferredoxin revealed negligible chemical shift changes in domain I, whereas much larger chemical shift changes were observed in domain II. The residues with larger chemical shift changes were located on the basic surface of domain II. Considering that ferredoxin is predominantly negatively charged, we propose the following hypothesis: First, an iron-sulphur cluster is assembled on domain I. Next, domain II interacts with the ferredoxin, thus tethering domain I close to the ferredoxin. Finally, domain I transfers the iron-sulphur cluster to the ferredoxin. Thus, domain II facilitates the efficient transfer of the iron-sulphur cluster from domain I to the ferredoxin.

PubMed: 17545250
DOI: 10.1093/jb/mvm120

実験手法

SOLUTION NMR