2OT2

Solution Structure of HypC

2OT2 の概要

• エントリーDOI: 10.2210/pdb2ot2/pdb
• NMR情報: BMRB: 15152
• 分子名称: Hydrogenase isoenzymes formation protein hypC (1 entity in total)
• 機能のキーワード: beta barrel, chaperone
• 由来する生物種: Escherichia coli K12
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9738.96

構造登録者

Wang, L.,Jin, C. (登録日: 2007-02-07, 公開日: 2007-09-04, 最終更新日: 2024-05-29)

主引用文献

Wang, L.,Xia, B.,Jin, C.
Solution structure of Escherichia coli HypC
Biochem.Biophys.Res.Commun., 361:665-669, 2007

PubMed Abstract: Escherichia coli HypC plays an important role in the maturation process of the pre-maturated HycE, the large subunit of hydrogenase 3. It serves as an iron transfer as well as a chaperone protein during the maturation process of pre-HycE, and interacts with both HypD and HycE. The N-terminal cysteine residue of HypC plays a key role in the protein-protein interactions. Here, we present the three-dimensional structure of E. coli HypC, the first solution structure of HupF/HypC family. Our result demonstrates that E. coli HypC consists of a typical OB-fold beta-barrel with two C-terminal helixes. Sequence alignment and structural comparison reveal that the hydrophobic region on the surface of E. coli HypC, as well as the highly flexible C-terminal helixes, may involve in the interactions of E. coli HypC with other proteins.

PubMed: 17669368
DOI: 10.1016/j.bbrc.2007.07.094

実験手法

SOLUTION NMR