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. 1971 Aug;68(8):1853–1857. doi: 10.1073/pnas.68.8.1853

Structure of Concanavalin A at 4 Å Resolution

Florante A Quiocho *, George N Reeke Jr †, Joseph W Becker †, William N Lipscomb *, Gerald M Edelman †
PMCID: PMC389307  PMID: 5288772

Abstract

Concanavalin A, a phytohemagglutinin isolated from the jack bean, crystallizes at pH 6.8 in the orthorhombic space group 1222 with a = 89.9, b = 87.2, and c = 63.1 Å. We have analyzed x-ray diffraction intensity data to 4 Å resolution on native concanavalin A and five heavy-metal derivatives: lead, mersalyl, chloroplatinate, uranyl, and o-mercuri-p-nitrophenol. Heavy-atom positions, occupancies, and isotropic thermal parameters have been refined by least-squares methods.

The electron density maps clearly show the molecular shape and the packing of the concanavalin A molecules. The asymmetric unit (mol wt 27,000) forms an elliptical dome or “gumdrop” with a base of approximately 46 × 26 Å and a height of 42 Å. The subunits are paired across 2-fold axes parallel to the c-axis to form dimers. The dimers are in turn paired across points of D2 symmetry to form tetramers of roughly tetrahedral shape. Each unit has a depression located on the surface which could be the site of saccharide binding. In many regions we have been able to trace the course of the polypeptide chain.

Keywords: x-ray diffraction, heavy-atom derivatives, lectins

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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