1BQ0

J-DOMAIN (RESIDUES 1-77) OF THE ESCHERICHIA COLI N-TERMINAL FRAGMENT (RESIDUES 1-104) OF THE MOLECULAR CHAPERONE DNAJ, NMR, 20 STRUCTURES

1BQ0 の概要

• エントリーDOI: 10.2210/pdb1bq0/pdb
• NMR情報: BMRB: 4228
• 分子名称: DNAJ (1 entity in total)
• 機能のキーワード: chaperone, heat shock, protein folding, dnak
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm: P08622
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11417.55

構造登録者

Huang, K.,Flanagan, J.M.,Prestegard, J.H. (登録日: 1998-08-20, 公開日: 1999-06-15, 最終更新日: 2024-05-22)

主引用文献

Huang, K.,Flanagan, J.M.,Prestegard, J.H.
The influence of C-terminal extension on the structure of the "J-domain" in E. coli DnaJ.
Protein Sci., 8:203-214, 1999

PubMed Abstract: Two different recombinant constructs of the N-terminal domain in Escherichia coli DnaJ were uniformly labeled with nitrogen-15 and carbon-13. One, DnaJ(1-78), contains the complete "J-domain," and the other, DnaJ(1-104), contains both the "J-domain" and a conserved "G/F" extension at the C-terminus. The three-dimensional structures of these proteins have been determined by heteronuclear NMR experiments. In both proteins the "J-domain" adopts a compact structure consisting of a helix-turn-helix-loop-helix-turn-helix motif. In contrast, the "G/F" region in DnaJ(1-104) does not fold into a well-defined structure. Nevertheless, the "G/F" region has been found to have an effect on the packing of the helices in the "J-domain" in DnaJ(1-104). Particularly, the interhelical angles between Helix IV and other helices are significantly different in the two structures. In addition, there are some local conformational changes in the loop region connecting the two central helices. These structural differences in the "J-domain" in the presence of the "G/F" region may be related to the observation that DnaJ (1-78) is incapable of stimulating the ATPase activity of the molecular chaperone protein DnaK despite evidence that sites mediating the binding of DnaJ to DnaK are located in the 1-78 segment.

PubMed: 10210198

実験手法

SOLUTION NMR