2LTN

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

Summary for 2LTN

• Entry DOI: 10.2210/pdb2ltn/pdb
• Descriptor: PEA LECTIN, ALPHA CHAIN, PEA LECTIN, BETA CHAIN, MANGANESE (II) ION, ... (5 entities in total)
• Functional Keywords: lectin
• Biological source: Pisum sativum (pea); More
• Total number of polymer chains: 4
• Total formula weight: 51384.36

Authors

Suddath, F.L.,Phillips, S.R.,Einspahr, H. (deposition date: 1990-06-26, release date: 1990-07-15, Last modification date: 2024-02-21)

Primary citation

Prasthofer, T.,Phillips, S.R.,Suddath, F.L.,Engler, J.A.
Design, expression, and crystallization of recombinant lectin from the garden pea (Pisum sativum).
J.Biol.Chem., 264:6793-6796, 1989

PubMed Abstract: 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.

PubMed: 2708344

Experimental method

X-RAY DIFFRACTION (1.7 Å)