1fat

From Proteopedia

Revision as of 14:06, 5 November 2007

PHYTOHEMAGGLUTININ-L

Overview

The structure of phytohemagglutinin-L (PHA-L), a leucoagglutinating seed, lectin from Phaseolus vulgaris, has been solved with molecular replacement, using the coordinates of lentil lectin as model, and refined at a, resolution of 2.8 A. The final R-factor of the structure is 20.0%. The, quaternary structure of the PHA-L tetramer differs from the structures of, the concanavalin A and peanut lectin tetramers, but resembles the, structure of the soybean agglutinin tetramer. PHA-L consists of two, canonical legume lectin dimers that pack together through the formation of, a close contact between two beta-strands. Of the two covalently bound, oligosaccharides per monomer, only one GlcNAc residue per monomer is, visible in the electron density. In this article we describe the structure, of PHA-L, and we discuss the putative position of the high affinity, adenine-binding site present in a number of legume lectins. A comparison, with transthyretin, a protein that shows a remarkable resemblance to, PHA-L, gives further ground to our proposal.

About this Structure

1FAT is a Single protein structure of sequence from Phaseolus vulgaris with NAG, MN and CA as ligands. Structure known Active Sites: CAA, CAB, CAC, CAD, MNA, MNB, MNC and MND. Full crystallographic information is available from OCA.

Reference

The crystallographic structure of phytohemagglutinin-L., Hamelryck TW, Dao-Thi MH, Poortmans F, Chrispeels MJ, Wyns L, Loris R, J Biol Chem. 1996 Aug 23;271(34):20479-85. PMID:8702788

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