Preliminary crystallographic studies of triosephosphate isomerase (TIM) from the hyperthermophilic Archaeon <i>Pyrococcus woesei</i>

Bell, G.; Russell, Rosemary; Kohlhoff, Michael; Hensel, Reinhard; Danson, Michael J.; Hough, David W.; Taylor, G.L.

doi:10.1107/s0907444998004910

Cited by 13 publications

(8 citation statements)

References 16 publications

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“…Two other hyperthermophilic archaeal TIMs were reported to exist also in a tetrameric form 42, 43. Also, various other enzymes from thermophilic and hyperthermophilic enzymes are known to exist as higher‐order association states compared with their mesophilic analogues, suggesting that the formation of higher‐order oligomers is one way by which hyperthermostability is achieved in nature 1…”

Section: Resultsmentioning

confidence: 99%

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

et al. 1999

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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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Section: Resultsmentioning

confidence: 99%

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

et al. 1999

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show abstract

“…Two other hyperthermophilic archaeal TIMs were reported to exist also in a tetrameric form. 42,43 Also, various other enzymes from thermophilic and hyperthermophilic enzymes are known to exist as higher-order association states compared with their mesophilic analogues, suggesting that the formation of higher-order oligomers is one way by which hyperthermostability is achieved in nature. 1…”

Section: Tetramerizationmentioning

confidence: 99%

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

Maes¹,

Zeelen²,

Thanki³

et al. 1999

Proteins

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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 hyperthermo-philes. 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 ther-mophilic TIMs, the highest amount of accessible hydrophobic surface is buried during the folding and assembly process. Proteins 1999;37:441-453. 1999 Wiley-Liss, Inc.

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“…TIM activity has been detected in crude extracts of many archaeal species (40-42, 70, 105, 128), and TIM sequences have been identified in apparently all archaeal genomes (36,43 (145)(146)(147)(148). The archaeal TIM sequences are shorter, by ϳ20 amino acids, than those of their bacterial/eukaryotic counterparts, comprising ϳ230 amino acids and ϳ250 to 260 amino acids, corresponding to ϳ24 kDa and 28 kDa, respectively (36,139).…”

Section: Triosephosphate Isomerasementioning

confidence: 99%

Carbohydrate Metabolism in Archaea: Current Insights into Unusual Enzymes and Pathways and Their Regulation

Bräsen

Esser

Rauch

et al. 2014

Microbiol Mol Biol Rev

271

294

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SUMMARY The metabolism of Archaea , the third domain of life, resembles in its complexity those of Bacteria and lower Eukarya . However, this metabolic complexity in Archaea is accompanied by the absence of many “classical” pathways, particularly in central carbohydrate metabolism. Instead, Archaea are characterized by the presence of unique, modified variants of classical pathways such as the Embden-Meyerhof-Parnas (EMP) pathway and the Entner-Doudoroff (ED) pathway. The pentose phosphate pathway is only partly present (if at all), and pentose degradation also significantly differs from that known for bacterial model organisms. These modifications are accompanied by the invention of “new,” unusual enzymes which cause fundamental consequences for the underlying regulatory principles, and classical allosteric regulation sites well established in Bacteria and Eukarya are lost. The aim of this review is to present the current understanding of central carbohydrate metabolic pathways and their regulation in Archaea . In order to give an overview of their complexity, pathway modifications are discussed with respect to unusual archaeal biocatalysts, their structural and mechanistic characteristics, and their regulatory properties in comparison to their classic counterparts from Bacteria and Eukarya . Furthermore, an overview focusing on hexose metabolic, i.e., glycolytic as well as gluconeogenic, pathways identified in archaeal model organisms is given. Their energy gain is discussed, and new insights into different levels of regulation that have been observed so far, including the transcript and protein levels (e.g., gene regulation, known transcription regulators, and posttranslational modification via reversible protein phosphorylation), are presented.

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Preliminary crystallographic studies of triosephosphate isomerase (TIM) from the hyperthermophilic Archaeon Pyrococcus woesei

Cited by 13 publications

References 16 publications

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

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

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

Carbohydrate Metabolism in Archaea: Current Insights into Unusual Enzymes and Pathways and Their Regulation

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