Localized structural effects of electrostatic interactions in a thermostable enzyme.

@article{Rhode1999LocalizedSE,
  title={Localized structural effects of electrostatic interactions in a thermostable enzyme.},
  author={David J. Rhode and Bruce L. Martin},
  journal={Biochemical and biophysical research communications},
  year={1999},
  volume={258 1},
  pages={
          179-83
        }
}
  • D. J. Rhode, B. Martin
  • Published 29 April 1999
  • Chemistry, Medicine
  • Biochemical and biophysical research communications
The sequence and resolved structure of thermotrophic isopropylmalate dehydrogenase (IPMDH) and a related protein, mesotrophic isocitrate dehydrogenase (IDH), were compared emphasizing clusters of charged residues identified from X-ray crystallographic studies (Wallon, G., Kryger, G., Lovett, S. T., Oshima, T., Ringe, D., and Petsko, G. A. (1997) J. Mol. Biol. 266, 1016-1031). Mesotrophic isocitrate dehydrogenase was used for comparison because crystallographic data for a mesotrophic form of… Expand
Crystal structures of 3-isopropylmalate dehydrogenases with mutations at the C-terminus: crystallographic analyses of structure-stability relationships.
TLDR
It is shown that the active-site cleft can be regulated by open-close movement of the minor groove located at the opposite side to the active -site groove on the same subunit, through a paperclip-like motion. Expand
Domain Motion in 3-isopropylmalate dehydrogenase: A Strategy to Enhance its Thermal Stability
In order to elucidate the thermal properties of Thermus thermophilus 3-isopropylmalate dehydrogenase, mutant structures with mutations at the C- terminus were compared with each other. The structuralExpand
Understanding thermostability in cytochrome P450 by combinatorial mutagenesis
  • S. Maves, S. Sligar
  • Biology, Medicine
  • Protein science : a publication of the Protein Society
  • 2001
TLDR
A randomized library of point mutants was generated and it was suggested that electrostatic interactions involving salt links and charge–charge interactions, as well as contributions from other interactions such as aromatic stacking, and side chain volume of hydrophobic residues contribute to enhanced thermostability in this cytochrome P450. Expand
Rates of unfolding, rather than refolding, determine thermal stabilities of thermophilic, mesophilic, and psychrotrophic 3-isopropylmalate dehydrogenases.
TLDR
Comparative experimental unfolding-refolding studies of the three IPMDHs with different thermostabilities have revealed a close relationship between thermostability and unfolding rate, dictated by global structural characteristics rather than by thermodynamic stability. Expand

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To reveal the structural basis of the increased thermal stability of 3-isopropylmalate dehydrogenase (IPMDH) from Thermus thermophilus, an extreme thermophile, the homology-based structural model ofExpand
Hydrophobic interaction at the subunit interface contributes to the thermostability of 3-isopropylmalate dehydrogenase from an extreme thermophile, Thermus thermophilus.
TLDR
The cloned and sequenced the leuB gene encoding 3-isopropylmalate dehydrogenase from Escherichia coli K-12 and the resulted mutant enzyme was more resistant to heat than the wild-type enzyme. Expand
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The results of this analysis indicate that the ion-pair networks become more fragmented as the temperature stability of the enzyme decreases and are consistent with a role for the involvement of such networks in the adaptation of enzymes to extreme temperatures. Expand
Crystal structures of Escherichia coli and Salmonella typhimurium 3-isopropylmalate dehydrogenase and comparison with their thermophilic counterpart from Thermus thermophilus.
TLDR
The basis of protein stability has been investigated by the structural comparison of themophilic enzymes with their mesophilic counterparts, and a mutant that created a cavity in the hydrophobic core of the thermophilic enzyme was designed to investigate the importance of packing density for thermostability. Expand
Sequence and homology model of 3-isopropylmalate dehydrogenase from the psychrotrophic bacterium Vibrio sp. I5 suggest reasons for thermal instability.
TLDR
Three recently solved homologous isopropylmalate dehydrogenase crystal structures from thermophilic and mesophilic organisms have been used to build a homology model for the psychrotrophic IPMDH and to deduce the possible structural reasons for its decreased thermostability. Expand
Effect of polar side chains at position 172 on thermal stability of 3‐isopropylmalate dehydrogenase from Thermus thermophilus
To understand the role of the amino acid residue at position 172 in the conformational stability, four mutant enzymes of Thermus thermophilus 3‐isopropylmalate dehydrogenase in which Ala172 wasExpand
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The effects of temperature and SDS on the three-dimensional organization and secondary structure of beta-glycosidase from the thermophilic archaeon Sulfolobus solfataricus were investigated by CD, IRExpand
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The detailed knowledge of the stability-determining region of TLP-ste permits effective rational design of stabilizing mutations, which, presumably, are also useful for related TLP such as thermolysin. Expand
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NADP-dependent isocitrate dehydrogenase (EC 1.1.1.42) was purified to electrophoretic homogeneity from an extremely thermophilic bacterium, Thermus thermophilus HB8, and shown to be a dimeric proteinExpand
Crystallization and preliminary X-ray studies of isocitrate dehydrogenase from Thermus thermophilus HB8.
TLDR
Isocitrate dehydrogenase from the thermophilic bacterium, Thermus thermophilus HB8, was crystallized by the vapor diffusion hanging drop method with polyethylene glycol 6000 as the precipitant to identify the orthorhombic crystals. Expand
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