2ltn | pdb_00002ltn

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

spinqualitylabelsall models 2ltn, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2ltn is a 4 chain structure with sequence from Garden pea. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, MN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [LEC_PEA] D-mannose specific lectin. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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