Crystallization and crystal data of thaumatin I, a sweet‐tasting protein from <i>Thaumatococcus daniellii</i> benth

Wel, H. van der; Soest, T. C. van; Royers, E.C.

doi:10.1016/0014-5793(75)81117-3

Cited by 27 publications

(12 citation statements)

References 5 publications

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“…We have subsequently found a new crystallization condition that made it possible to obtain many heavy atom derivatives. The new crystal form has the same space group as the previous one (9) with 50o of the crystal volume being solvent. X-ray diffraction data were collected at 40C on a Nicolet four-circle automatic diffractometer modified with an extended detector arm and helium-filled incident and diffracted beam collimators.…”

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

Three-dimensional structure of thaumatin I, an intensely sweet protein.

Vos¹,

Hatada²,

Wel³

et al. 1985

Proc. Natl. Acad. Sci. U.S.A.

120

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Thaumatin and monellin are the two sweetest compounds known to man-about 100,000 times sweeter than sugar on a molar basis and 3000 times on a weight basis. These proteins represent a unique class of proteins that are tasteactive. We report the three-dimensional structure of thaumatin I at 3.1 A resolution.Taste is one of the least understood senses from a biochemical point of view. Sweet taste can be elicited to varying degrees by a wide variety of compounds in high concentration, such as mono-and disaccharides, several amino acids, dipeptide derivatives, glycerol, cyclamates, saccharine, acesulfame, some hydrated inorganic compounds, and others.Sensations of sweet taste are elicited by sweet compounds binding to sweet receptors of taste buds on the tongue, similar to hormone-hormone receptor binding. However, the similarity ends here. A 50% binding of hormone receptors usually occurs at around 10-8 to 10-11 M concentration of hormones, but in the case of sweet receptors the concentration to register sweet taste is about 10-1 to 10-3 M of sucrose. Furthermore, like other sensory perceptions, taste is associated with a unique set of sensation parameters. These are threshold concentration, onset time, intensity, saturation concentration, lingering time, aftertaste, and potentiation of other tastes or flavors. Systematic studies of these properties of taste-active compounds have been difficult in the past because of high levels of nonspecific binding between the sweet comnpounds and the sweet receptors due to the high concentrations of the sweet compounds required to elicit the sweet taste.One of the most interesting and unusual recent findings is the existence of two intensely sweet proteins, monellin and thaumatin (for a recent review, see ref. 1). The sweet taste of the proteins can be registered at a very low concentration (10' M), comparable to those in hormone-hormone receptor interaction. These proteins are about 100,000 times sweeter than sucrose on a molar basis and several thousand times sweeter on a weight basis. In fact, these two proteins are the two sweetest compounds known to man. With these proteins, studies similar to those performed for hormonehormone receptors can be initiated. Three-dimensional structures of these proteins are likely to provide a solid foundation upon which studies to understand the molecular basis of sweet taste can be designed. We here report the crystal structure of thaumatin I at 3.1 A resolution.Thaumatins have been isolated from the fruit of a West African rain forest shrub, Thaumatococcus daniellii Benth (2), which has been used for centuries by inhabitants of the region to sweeten foods such as bread and palm wine, There are two major sweet proteins in the fruit, thaumatin I and II, with almost identical molecular weights of 22,000. They consist of 207 amino acids and have identical amino acid sequences except for five residues (3, 4). There are no histidine residues, but there are eight disulfide bonds. Partially pure thaumatin is available commercially from Si...

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Section: Methodsmentioning

confidence: 99%

“…Thaumatin I has been crystallized in two different crystalline forms (9). Both crystalline forms are unstable in most heavy atom soaking conditions (unpublished results).…”

Section: Methodsmentioning

confidence: 99%

Three-dimensional structure of thaumatin I, an intensely sweet protein.

Vos¹,

Hatada²,

Wel³

et al. 1985

Proc. Natl. Acad. Sci. U.S.A.

120

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“…The third, tetragonal crystal form was found in crystals grown by vapour-diffusion method in the presence of 1 M sodium potassium tartrate containing 0.1 M ADA (sodium-N-2-acetamido-iminodiacetic acid) at pH 6.5 [2]. These crystals were similar to one grown from ammonium sulphate solution [18]. Thaumatin has also been crystallized in hexagonal crystal form from a tartrate and glycerol containing solution after shifting temperature from 293 to 277 K [17,[19][20][21].…”

Section: Analysis Of Thaumatin Crystallization Realized By Cu 2+ Co-cmentioning

confidence: 98%

“…Previously thaumatin has been crystallized in four different forms: orthorhombic (1.75 Å ), monoclinic (2.60 Å ), tetragonal (1.75 Å ) and hexagonal (1.60 Å ) [2,4,5,17,18]. Orthorhombic and monoclinic crystal forms were obtained by using hanging-drop vapour-diffusion method from PEG as a precipitating agent [4,5,12].…”

Section: Analysis Of Thaumatin Crystallization Realized By Cu 2+ Co-cmentioning

confidence: 99%

Copper co-crystallization and divalent metal salts cross-influence effect: A new optimization tool improving crystal morphology and diffraction quality

Tomčová

Smatanová

2007

Journal of Crystal Growth

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“…This protein family includes the sweet-tasting thaumatin from Thaumatococcus danielli (Van der Wel et al, 1975), the bifunctional maize a-amylase/trypsin inhibitor (Richardson et al, 1987), the salt-induced protein NP24 from tomato (King et al, 1988), osmotin from tobacco (Singh et al, 1989), and the PR-protein from tobacco (Cornelissen et al, 1986). TLPs are synthesized by plants in response to pathogen infection and known as an antifungal compound.…”

Section: Introductionmentioning

confidence: 99%

In vitro and in planta Interaction Evidence between Nicotiana tabacum Thaumatin-Like Protein 1 (TLP1) and Cucumber mosaic virus Proteins

et al. 2005

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Using a yeast two-hybrid system, we identified a plant cellular factor that interacts with the proteins of the Cucumber mosaic virus (CMV). Initially 14 candidate genes were isolated from Nicotiana tabacum, using a full-length CMV 1a gene as bait. Among the candidate genes, two were encoding thaumatin-like proteins (TLP), and were designated as Nicotiana tabacum thaumatin-like protein 1 (NtTLP1). Consistent with this observation, recombinant GST-NtTLP1 protein, which was expressed and purified in E. coli, bound tightly to CMV 1a in vitro. In planta interaction was also verified via co-immunoprecipitation. Additionally, NtTLP1 specifically interacted with the CMV movement-related proteins, movement protein and coat protein, in yeast. Real-time quantitative reverse transcription-polymerase chain reaction (RT-PCR) analysis showed that the expression of NtTLP1 increased as the result of CMV inoculation.

show abstract

Crystallization and crystal data of thaumatin I, a sweet‐tasting protein from Thaumatococcus daniellii benth

Cited by 27 publications

References 5 publications

Three-dimensional structure of thaumatin I, an intensely sweet protein.

Three-dimensional structure of thaumatin I, an intensely sweet protein.

Copper co-crystallization and divalent metal salts cross-influence effect: A new optimization tool improving crystal morphology and diffraction quality

In vitro and in planta Interaction Evidence between Nicotiana tabacum Thaumatin-Like Protein 1 (TLP1) and Cucumber mosaic virus Proteins

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