Structural characterization of a methionine-rich, emulsifying protein from sunflower seed

Pandya, Maya J.; Sessions, Richard B.; Williams, Phil B.; Dempsey, Christopher E.; Tatham, Arthur S.; Shewry, Peter R.; Clarke, Anthony R.

doi:10.1002/(sici)1097-0134(20000215)38:3<341::aid-prot9>3.0.co;2-d

Cited by 27 publications

(10 citation statements)

References 39 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The homology model of the C‐terminal domain of M. grisea ( M. grisea ‐C) was built on the Δ‐9 desaturase protein (1afr) according to the alignment in Fig. 2, using standard methods [23]. A substrate complex was generated by constraining an oxygen molecule to lie between the two Fe ions to give a μ‐1,2 peroxo complex, then ubiquinol was docked into the active site such that the aromatic ring of the ligand lay over the di‐iron centre.…”

Section: Methodsmentioning

confidence: 99%

New sequence data enable modelling of the fungal alternative oxidase and explain an absence of regulation by pyruvate

et al. 2000

View full text Add to dashboard Cite

Respiratory rates involving the alternative oxidase (AO) were studied in mitochondria from Tapesia acuformis. There was no evidence for regulation by pyruvate, in contrast with plant AO. The site of interaction of pyruvate with the plant AO is a conserved cysteine. The primary sequence was obtained for AO from Magnaporthe grisea and compared with four published sequences for fungal AO. In all cases this cysteine was absent. Sequence data were obtained for the C-terminal domain of a further five fungal AOs. In this region the fungal sequences were all consistent with a four-helix, di-iron binding structure as in the ferritin-fold family. A molecular model of this domain was deduced from the structure of v v-9 desaturase. This is in general agreement with that developed for plant AOs, despite very low sequence identity between the two kingdoms. Further modelling indicated an appropriate active site for binding of ubiquinol, required in the AO redox reaction. ß

show abstract

Section: Methodsmentioning

confidence: 99%

New sequence data enable modelling of the fungal alternative oxidase and explain an absence of regulation by pyruvate

et al. 2000

View full text Add to dashboard Cite

show abstract

“…Fourier transform infrared (FT-IR) spectroscopic and/or circular dichroism (CD) studies have demonstrated that 2S albumins from many plant species, including those from yellow mustard [27], rapeseed [28-30], radish ( Raphanus sativus ) [31], sunflower [32-34], Brazil nut [19, 34], peanut ( Arachis hypogea ) [35, 36], soybean ( Glycine max .) [37], sesame [25] and oriental mustard [38] are rich in α-helix contents (35-50 %).…”

Section: Structural Features Of 2s Albuminsmentioning

confidence: 99%

2S Albumin Storage Proteins: What Makes them Food Allergens?

Moreno¹,

Clemente²

2008

Open Biochem J

196

210

View full text Add to dashboard Cite

2S albumin storage proteins are becoming of increasing interest in nutritional and clinical studies as they have been reported as major food allergens in seeds of many mono- and di-cotyledonous plants. This review describes the main biochemical, structural and functional properties of these proteins thought to play a role in determining their potential allergenicity. 2S albumins are considered to sensitize directly via the gastrointestinal tract (GIT). The high stability of their intrinsic protein structure, dominated by a well-conserved skeleton of cysteine residues, to the harsh conditions present in the GIT suggests that these proteins are able to cross the gut mucosal barrier to sensitize the mucosal immune system and/or elicit an allergic response. The flexible and solvent-exposed hypervariable region of these proteins is immunodominant and has the ability to bind IgE from allergic patients´ sera. Several linear IgE-binding epitopes of 2S albumins spanning this region have been described to play a major role in allergenicity; the role of conformational epitopes of these proteins in food allergy is far from being understood and need to be investigated. Finally, the interaction of these proteins with other components of the food matrix might influence the absorption rates of immunologically reactive 2S albumins but also in their immune response.

show abstract

“…SFAs are basic proteins (average isoelectric pH of about 8.8) with molecular weights ranging from 10 to 18 kDa 137–141. Two types of SFAs are distinguished: methionine‐rich and methionine‐poor albumins 140–142. In contrast to 2S seed albumins from other species that consist of two chains linked by disulfide bonds, SFAs consist of a single polypeptide chain 137, 143–146.…”

Section: Sunflower Albuminsmentioning

confidence: 99%

“…The latter is called SFA 8 based on its order of elution in RP‐HPLC138 and contains an unusually high proportion of hydrophobic residues and a large amount of S‐containing amino acids: 16 methionines and eight cysteines. Molecular modelling studies predict that SFA 8 has a compact structure with hydrophobic residues clustered to form a large hydrophobic face 142. SFA 8 together with a protein called SFA 7 may account for about 10–20% of the total sunflower albumins 106.…”

Section: Sunflower Albuminsmentioning

confidence: 99%

Sunflower proteins: overview of their physicochemical, structural and functional properties

2007

View full text Add to dashboard Cite

There is increasing worldwide demand for proteins of both animal and plant origin. However, animal proteins are expensive in terms of both market price and environmental impact. Among alternative plant proteins, sunflower seeds are particularly interesting in view of their widespread availability in areas where soy is not or only sparsely produced. Compared with other sources of vegetable proteins, sunflower seeds have been reported to have a low content of antinutritional factors. Although the absence of these factors is important, the functionality of the protein preparations will mainly determine their applicability. This review provides detailed information about sunflower seed composition and processing, including processes to remove phenolic compounds from meals. The main part of the review concerns the structure and functionality of the two major protein fractions, helianthinin and 2S albumins. Regarding functionality, emphasis is on solubility, thermal behaviour and surface activity. Protein structure and functionality are discussed as a function of extrinsic factors such as pH, ionic strength, temperature and the presence of other seed components, particularly chlorogenic acid. In addition, sunflower proteins are compared from a structural and functional point of view with other plant proteins, particularly soy proteins.

show abstract

Structural characterization of a methionine-rich, emulsifying protein from sunflower seed

Cited by 27 publications

References 39 publications

New sequence data enable modelling of the fungal alternative oxidase and explain an absence of regulation by pyruvate

New sequence data enable modelling of the fungal alternative oxidase and explain an absence of regulation by pyruvate

2S Albumin Storage Proteins: What Makes them Food Allergens?

Sunflower proteins: overview of their physicochemical, structural and functional properties

Contact Info

Product

Resources

About