1bq0
From Proteopedia
|
J-DOMAIN (RESIDUES 1-77) OF THE ESCHERICHIA COLI N-TERMINAL FRAGMENT (RESIDUES 1-104) OF THE MOLECULAR CHAPERONE DNAJ, NMR, 20 STRUCTURES
Overview
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.
About this Structure
1BQ0 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
The influence of C-terminal extension on the structure of the "J-domain" in E. coli DnaJ., Huang K, Flanagan JM, Prestegard JH, Protein Sci. 1999 Jan;8(1):203-14. PMID:10210198
Page seeded by OCA on Tue Nov 20 11:49:33 2007
