Biochemical and crystallographic data for phaseolin, the storage protein from Phaseolus vulgaris

Abstract

We have isolated and biochemically characterized a major seed protein from Phaseolus vulgaris (common garden green bean) that appears to be identical with a form of the storage protein of that plant seed known as phaseolin. We have further shown that it appears very similar in most properties to the storage protein from Canavalia ensiformis (jack bean) which we have solved to 3.0-A resolution using X-ray diffraction techniques. [McPherson, A., & Rich, A. (1973) J. Biochem. (Tokyo) 74, 155-160; McPherson, A., & Spencer, R. (1975) Arch. Biochem. Biophys. 169, 650-661; McPherson, A. (1980) J. Biol. Chem. 255, 10472-10480]. We have crystallized phaseolin and conducted a preliminary X-ray diffraction analysis on it as well. The data show the crystals to be of pseudo cubic space group P432, although the symmetry can be, strictly speaking, only P1. The unit cell has one trimeric molecule of 150 000 daltons in a unit cell of dimensions a = b = c = 66.6 and alpha = beta = gamma = 90 degrees. The crystals apparently possess some form of disorder that makes reconciliation of the unit cell contents with the observed crystallographic properties difficult, although they do diffract strongly to better than 2.8-A resolution. No evidence of twinning has been observed.

Fennel Waste-Based Films Suitable for Protecting Cultivations

“…In fact, it is possible to observe the presence of phaseolin crystals of quasi-cubic symmetry on the surface of the film containing unmodified phaseolin. These crystal morphologies are common to a large number of other varieties of seed-storage proteins when extracted under acidic conditions . Interestingly, SEM revealed that, in the film obtained in the presence of TG, phaseolin crystals are not evident, suggesting that the action of the enzyme on the globular protein affects its 3D structure.…”

Substrate Specificity of a Novel Serine Protease from Soybean [Glycine max (L.) Merrill]

“…It is very interesting that the & preparation modified by limited proteolysis was more easily crystallized than the native /%. The previous investigations on two vitellins, canavalin from jack bean and phaseolin from French bean, showed that these two storage proteins were cleaved specifically at a single site between two major domains with retention of the quaternary structures of the vicillin trimers, and the products could be crystallized more easily than the native proteins (22,23). The cleaved site on the /?…”

Ensuring Global Food Security by Improving Protein Content in Major Grain Legumes Using Breeding and ‘Omics’ Tools

“…Common bean ( Phaseolous vulgaris L.) SPC ranges from 20 to 30% [ 25 , 26 ], and plays a pivotal role in mitigating protein-related malnutrition, especially in underdeveloped countries [ 46 , 47 ]. The major storage protein in common bean is phaseolin, accounting for 36–46% of total seed proteins [ 48 ], with 50–60% of the phaseolin belonging to the 7S vicilin class, insufficient in methionine, cysteine, and tryptophan essential amino acids [ 49 , 50 , 51 ].…”