The crystal structure of triosephosphate isomerase (TIM) from Thermotoga maritima: A comparative thermostability structural analysis of ten different TIM structures

Dominique Maes, Johan P. Zeelen, Narmada Thanki, Nicola Beaucamp, Marco Alvarez, Thi Minh Hoa Dao, Jan Backmann, Joseph A. Martial, Lode Wyns, Rainer Jaenicke, Rik K. Wierenga

Resultado de la investigación: Article

126 Citas (Scopus)

Resumen

The molecular mechanisms that evolution has been employing to adapt to environmental temperatures are poorly understood. To gain some further insight into this subject we solved the crystal structure of triosephosphate isomerase (TIM) from the hyperthermophilic bacterium Thermotoga maritima (TmTIM). The enzyme is a tetramer, assembled as a dimer of dimers, suggesting that the tetrameric wild-type phosphoglycerate kinase PGK-TIM fusion protein consists of a core of two TIM dimers covalently linked to 4 PGK units. The crystal structure of TmTIM represents the most thermostable TIM presently known in its 3D-structure. It adds to a series of nine known TIM structures from a wide variety of organisms, spanning the range from psychrophiles to hyperthermophiles. Several properties believed to be involved in the adaptation to different temperatures were calculated and compared for all ten structures. No sequence preferences, correlated with thermal stability, were apparent from the amino acid composition or from the analysis of the loops and secondary structure elements of the ten TIMs. A common feature for both psychrophilic and T. maritima TIM is the large number of salt bridges compared with the number found in mesophilic TIMs. In the two thermophilic TIMs, the highest amount of accessible hydrophobic surface is buried during the folding and assembly process.

Idioma originalEnglish
Páginas (desde-hasta)441-453
Número de páginas13
PublicaciónProteins: Structure, Function and Genetics
Volumen37
N.º3
DOI
EstadoPublished - 15 nov 1999

Huella dactilar

Thermotoga maritima
Triose-Phosphate Isomerase
Structural analysis
Crystal structure
Dimers
Phosphoglycerate Kinase
Temperature
Molecular Evolution
Bacteria
Thermodynamic stability
Fusion reactions
Salts
Hot Temperature
Amino Acids
Enzymes
Chemical analysis

ASJC Scopus subject areas

  • Genetics
  • Structural Biology
  • Biochemistry
  • Molecular Biology

Citar esto

Maes, Dominique ; Zeelen, Johan P. ; Thanki, Narmada ; Beaucamp, Nicola ; Alvarez, Marco ; Minh Hoa Dao, Thi ; Backmann, Jan ; Martial, Joseph A. ; Wyns, Lode ; Jaenicke, Rainer ; Wierenga, Rik K. / The crystal structure of triosephosphate isomerase (TIM) from Thermotoga maritima : A comparative thermostability structural analysis of ten different TIM structures. En: Proteins: Structure, Function and Genetics. 1999 ; Vol. 37, N.º 3. pp. 441-453.
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abstract = "The molecular mechanisms that evolution has been employing to adapt to environmental temperatures are poorly understood. To gain some further insight into this subject we solved the crystal structure of triosephosphate isomerase (TIM) from the hyperthermophilic bacterium Thermotoga maritima (TmTIM). The enzyme is a tetramer, assembled as a dimer of dimers, suggesting that the tetrameric wild-type phosphoglycerate kinase PGK-TIM fusion protein consists of a core of two TIM dimers covalently linked to 4 PGK units. The crystal structure of TmTIM represents the most thermostable TIM presently known in its 3D-structure. It adds to a series of nine known TIM structures from a wide variety of organisms, spanning the range from psychrophiles to hyperthermophiles. Several properties believed to be involved in the adaptation to different temperatures were calculated and compared for all ten structures. No sequence preferences, correlated with thermal stability, were apparent from the amino acid composition or from the analysis of the loops and secondary structure elements of the ten TIMs. A common feature for both psychrophilic and T. maritima TIM is the large number of salt bridges compared with the number found in mesophilic TIMs. In the two thermophilic TIMs, the highest amount of accessible hydrophobic surface is buried during the folding and assembly process.",
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The crystal structure of triosephosphate isomerase (TIM) from Thermotoga maritima : A comparative thermostability structural analysis of ten different TIM structures. / Maes, Dominique; Zeelen, Johan P.; Thanki, Narmada; Beaucamp, Nicola; Alvarez, Marco; Minh Hoa Dao, Thi; Backmann, Jan; Martial, Joseph A.; Wyns, Lode; Jaenicke, Rainer; Wierenga, Rik K.

En: Proteins: Structure, Function and Genetics, Vol. 37, N.º 3, 15.11.1999, p. 441-453.

Resultado de la investigación: Article

TY - JOUR

T1 - The crystal structure of triosephosphate isomerase (TIM) from Thermotoga maritima

T2 - A comparative thermostability structural analysis of ten different TIM structures

AU - Maes, Dominique

AU - Zeelen, Johan P.

AU - Thanki, Narmada

AU - Beaucamp, Nicola

AU - Alvarez, Marco

AU - Minh Hoa Dao, Thi

AU - Backmann, Jan

AU - Martial, Joseph A.

AU - Wyns, Lode

AU - Jaenicke, Rainer

AU - Wierenga, Rik K.

PY - 1999/11/15

Y1 - 1999/11/15

N2 - The molecular mechanisms that evolution has been employing to adapt to environmental temperatures are poorly understood. To gain some further insight into this subject we solved the crystal structure of triosephosphate isomerase (TIM) from the hyperthermophilic bacterium Thermotoga maritima (TmTIM). The enzyme is a tetramer, assembled as a dimer of dimers, suggesting that the tetrameric wild-type phosphoglycerate kinase PGK-TIM fusion protein consists of a core of two TIM dimers covalently linked to 4 PGK units. The crystal structure of TmTIM represents the most thermostable TIM presently known in its 3D-structure. It adds to a series of nine known TIM structures from a wide variety of organisms, spanning the range from psychrophiles to hyperthermophiles. Several properties believed to be involved in the adaptation to different temperatures were calculated and compared for all ten structures. No sequence preferences, correlated with thermal stability, were apparent from the amino acid composition or from the analysis of the loops and secondary structure elements of the ten TIMs. A common feature for both psychrophilic and T. maritima TIM is the large number of salt bridges compared with the number found in mesophilic TIMs. In the two thermophilic TIMs, the highest amount of accessible hydrophobic surface is buried during the folding and assembly process.

AB - The molecular mechanisms that evolution has been employing to adapt to environmental temperatures are poorly understood. To gain some further insight into this subject we solved the crystal structure of triosephosphate isomerase (TIM) from the hyperthermophilic bacterium Thermotoga maritima (TmTIM). The enzyme is a tetramer, assembled as a dimer of dimers, suggesting that the tetrameric wild-type phosphoglycerate kinase PGK-TIM fusion protein consists of a core of two TIM dimers covalently linked to 4 PGK units. The crystal structure of TmTIM represents the most thermostable TIM presently known in its 3D-structure. It adds to a series of nine known TIM structures from a wide variety of organisms, spanning the range from psychrophiles to hyperthermophiles. Several properties believed to be involved in the adaptation to different temperatures were calculated and compared for all ten structures. No sequence preferences, correlated with thermal stability, were apparent from the amino acid composition or from the analysis of the loops and secondary structure elements of the ten TIMs. A common feature for both psychrophilic and T. maritima TIM is the large number of salt bridges compared with the number found in mesophilic TIMs. In the two thermophilic TIMs, the highest amount of accessible hydrophobic surface is buried during the folding and assembly process.

KW - Hydrophobicity

KW - Hyperthermophile

KW - Psychrophile

KW - Salt bridges

KW - Thermophile

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JO - Proteins: Structure, Function and Bioinformatics

JF - Proteins: Structure, Function and Bioinformatics

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