The influence of C-terminal extension on the structure of the 'J- domain' in E. coli DnaJ

Kai Huang, John Flanagan, James H. Prestegard

Research output: Contribution to journalArticle

39 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)203-214
Number of pages12
JournalProtein Science
Volume8
Issue number1
StatePublished - Jan 23 1999

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F region
Escherichia coli
Helix-Turn-Helix Motifs
Biomolecular Nuclear Magnetic Resonance
Molecular Chaperones
Adenosine Triphosphatases
Proteins
Nitrogen
Carbon
Binding Sites
Nuclear magnetic resonance
Experiments
Protein Domains

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

Cite this

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title = "The influence of C-terminal extension on the structure of the 'J- domain' in E. coli DnaJ",
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.",
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The influence of C-terminal extension on the structure of the 'J- domain' in E. coli DnaJ. / Huang, Kai; Flanagan, John; Prestegard, James H.

In: Protein Science, Vol. 8, No. 1, 23.01.1999, p. 203-214.

Research output: Contribution to journalArticle

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AB - 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.

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