1gik

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Revision as of 13:58, 20 November 2007

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spinqualitylabelsall models 1gik, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

POKEWEED ANTIVIRAL PROTEIN FROM SEEDS

Overview

The crystal structure of pokeweed antiviral protein from seeds of, Phytolacca americana (PAP-S) was solved at 1.8A. PAP-S is a one-chain, ribosome-inactivating protein (RIP) and distinctively contains three, well-defined N-acetylglucosamines, each covalently linked to an asparagine, residue at positions, 10, 44, and 255, respectively. The high-resolution, structure clearly shows the three mono-sugars to have either an alpha- or, a beta-conformation. Two of sugars are located on the same side of the, molecule with the active pocket. Except one hydrogen bond, there are no, intermolecular interactions between the polypeptide chain and the sugars., Instead the sugar conformations appear to be stabilized by intermolecular, interactions. The sugar structure defined at high resolution provides a, structural basis for understanding their possible biological activity. The, structural comparisons of PAP-S with other PAPs reveal that the major, disparity of these homologous molecules is the different charge, distribution on the upper right side of the front side near the active, pocket. Based on the available structure of the 50S ribosomal subunit, the, possible interactions between PAPs and the ribosome are discussed.

About this Structure

1GIK is a Single protein structure of sequence from Phytolacca americana with NAG and NDG as ligands. Active as rRNA N-glycosylase, with EC number 3.2.2.22 Full crystallographic information is available from OCA.

Reference

Crystal structure of pokeweed antiviral protein with well-defined sugars from seeds at 1.8A resolution., Zeng ZH, He XL, Li HM, Hu Z, Wang DC, J Struct Biol. 2003 Feb;141(2):171-8. PMID:12615543

Page seeded by OCA on Tue Nov 20 16:05:26 2007