2ltn

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Image:2ltn.jpg

2ltn, resolution 1.7Å

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DESIGN, EXPRESSION, AND CRYSTALLIZATION OF RECOMBINANT LECTIN FROM THE GARDEN PEA (PISUM SATIVUM)

Overview

The propeptide form of the lectin from the garden pea (Pisum sativum agglutinin) has been expressed in Escherichia coli by attaching its cDNA to an inducible promoter. By a number of criteria, including the ability to form dimers, hemagglutination titer, Western blot, and enzyme-linked immunosorbent assay, the resulting propeptide molecule is virtually indistinguishable from the mature proteolytically processed lectin isolated from peas. Preliminary crystallization experiments using the recombinant propeptide lectin yield crystals in space group P2(1)2(1)2(1) with a = 64.8 A, b = 73.8 A, and c = 109.0 A (1 A = 0.1 nm) that diffract to 2.8-A resolution. This unit cell size is quite similar to the unit cell determined for native pea lectin, suggesting that the overall structure of the recombinant prolectin is virtually identical.

About this Structure

2LTN is a Protein complex structure of sequences from Pisum sativum with and as ligands. Full crystallographic information is available from OCA.

Reference

Design, expression, and crystallization of recombinant lectin from the garden pea (Pisum sativum)., Prasthofer T, Phillips SR, Suddath FL, Engler JA, J Biol Chem. 1989 Apr 25;264(12):6793-6. PMID:2708344

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