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1nio

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Revision as of 20:10, 20 November 2007 by OCA (Talk | contribs)
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Image:1nio.gif

1nio, resolution 2.00Å

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Crystal structure of beta-luffin, a ribosome inactivating protein at 2.0A resolution

Overview

The crystal structure of beta-luffin at 2.0 A resolution was solved by the, molecular-replacement method using polyalanyl trichosanthin as the search, model. The structure was refined with CNS1.1, giving R(work) = 0.162 and, R(free) = 0.204. The r.m.s.d.s of the bond lengths and bond angles are, 0.008 A and 1.3 degrees, respectively. The overall structure is similar to, those of other type I RIPs. Three N-acetylglucosamine (Nag) molecules are, linked to residues Asn2, Asn78 and Asn85 of the protein.

About this Structure

1NIO is a Single protein structure of sequence from Luffa aegyptiaca with NAG as ligand. Active as rRNA N-glycosylase, with EC number 3.2.2.22 Full crystallographic information is available from OCA.

Reference

Crystal structure of beta-luffin, a ribosome-inactivating protein, at 2.0 A resolution., Ma QJ, Li JH, Li HG, Wu S, Dong YC, Acta Crystallogr D Biol Crystallogr. 2003 Aug;59(Pt 8):1366-70. Epub 2003, Jul 23. PMID:12876337

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