Details

Autor(en) / Beteiligte

• Meehan, E J
• McDuffie, J
• Einspahr, H
• Bugg, C E
• Suddath, F L

Titel

The crystal structure of pea lectin at 6-A resolution

Ist Teil von

• The Journal of biological chemistry, 1982-11, Vol.257 (22), p.13278-13282

Ort / Verlag

United States: Elsevier Inc

Erscheinungsjahr

1982

Link zum Volltext

Quelle

MEDLINE

Beschreibungen/Notizen

• The three-dimensional crystal structure of the mitogenic lectin from the green pea (Pisum sativum) has been determined at 6-A resolution by x-ray diffraction methods. Pea lectin was isolated by use of affinity chromatography and was crystallized from polyethylene glycol solutions. Crystals of pea lectin are orthorhombic, space group P212121, and diffract to at least 1.2-A resolution. The unit cell dimensions are a = 50.85(5), b = 61.23(5), and c = 137.3(2) A. The calculated mass of protein per asymmetric unit is 49,000 daltons, and the crystals are 44% solvent by volume. There are two pea lectin monomers per crystallographic asymmetric unit. Diffractometer data were collected from a native crystal and from a single site uranyl heavy atom derivative crystal. The position of the uranium atom, determined from three-dimensional Patterson maps, was refined by least squares techniques (R index - 0.46 for centric data). A three-dimensional electron density map was calculated by use of phases determined by isomorphous-replacement and anomalous-dispersion contributions. The boundaries of the pea lectin molecule are clearly visible in the map. The molecule appears to be a dimer, roughly peanut-shaped, formed by the close association of the two monomer units. In shape and size, it bears a striking resemblance to the concanavalin A dimer, in which monomers combine to form a dimer-wide contiguous antiparallel pleated sheet.