1bq0

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[[Image:1bq0.gif|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bq0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bq0 OCA], [http://www.ebi.ac.uk/pdbsum/1bq0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bq0 RCSB]</span>
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'''J-DOMAIN (RESIDUES 1-77) OF THE ESCHERICHIA COLI N-TERMINAL FRAGMENT (RESIDUES 1-104) OF THE MOLECULAR CHAPERONE DNAJ, NMR, 20 STRUCTURES'''
'''J-DOMAIN (RESIDUES 1-77) OF THE ESCHERICHIA COLI N-TERMINAL FRAGMENT (RESIDUES 1-104) OF THE MOLECULAR CHAPERONE DNAJ, NMR, 20 STRUCTURES'''
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[[Category: Huang, K.]]
[[Category: Huang, K.]]
[[Category: Prestegard, J H.]]
[[Category: Prestegard, J H.]]
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[[Category: chaperone]]
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[[Category: Chaperone]]
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[[Category: dnak]]
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[[Category: Dnak]]
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[[Category: heat shock]]
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[[Category: Heat shock]]
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[[Category: protein folding]]
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[[Category: Protein folding]]
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Revision as of 08:48, 2 May 2008

Template:STRUCTURE 1bq0

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 Fri May 2 11:48:48 2008

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