The structure of a haemopexin-fold protein from cow pea (Vigna unguiculata) suggests functional diversity of haemopexins in plants.

The haemopexin fold is present in almost all life forms and is utilized for carrying out diverse physiological functions. The structure of CP4, a haemopexin-fold protein from cow pea (Vigna unguiculata), was determined at 2.1 Å resolution.

Crystal structure and functional insights of hemopexin fold protein from grass pea.

A regulatory protein from grass pea (Lathyrus sativus), LS-24, a close homolog of albumin 2 from garden pea (Pisum sativum) that is associated with polyamine biosynthesis, was characterized and the structure of a hemopexin-type fold among plant proteins illustrated. Crystal structure of LS-24 determined at 2.2 A resolution by multiple isomorphous replacement phasing showed four-bladed beta-propeller structure having a pseudo 4-fold molecular symmetry along a metal ion-binding central channel.

Purification, identification and preliminary crystallographic characterization of a novel seed protein from Vigna unguiculata.

A tropical legume, Vigna unguiculata, was explored in order to identify potential allergens among the abundant seed proteins and to attempt their crystallographic study. Salt fractionation of the seed extract followed by chromatographic separation led to the purification of a 25 kDa protein. Gel-filtration chromatography of the 80% ammonium sulfate precipitation fraction led to separation of this protein in pure form, which was subjected to N-terminal sequencing.