1fat
From Proteopedia
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| , resolution 2.8Å | |||||||
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| Sites: | , , , , , , and | ||||||
| Ligands: | , and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Thu Mar 20 11:06:41 2008
Categories: Phaseolus vulgaris | Single protein | Hamelryck, T. | Loris, R. | CA | MN | NAG | Glycoprotein | Lectin | Plant defense protein
