2gmm

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(New page: 200px<br /><applet load="2gmm" size="350" color="white" frame="true" align="right" spinBox="true" caption="2gmm, resolution 2.15&Aring;" /> '''Metal-free (apo) P. ...)
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Revision as of 18:03, 29 January 2008


2gmm, resolution 2.15Å

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Metal-free (apo) P. angolensis seed lectin in complex with Man-alpha(1-2)Man

Overview

The interplay between metal binding, carbohydrate binding activity, stability and structure of the lectin from Pterocarpus angolensis was, investigated. Removal of the metals leads to a more flexible form of the, protein with significantly less conformational stability. Crystal, structures of this metal-free form show significant structural, rearrangements, although some structural features that allow the binding, of sugars are retained. We propose that substitution of an asparagine, residue at the start of the C-terminal beta-strand of the legume lectin, monomer hinders the trans-isomerization of the cis-peptide bond upon, demetallization and constitutes an intramolecular switch governing the, isomer state of the non-proline bond and ultimately the lectin phenotype.

About this Structure

2GMM is a Single protein structure of sequence from Pterocarpus angolensis with as ligand. Full crystallographic information is available from OCA.

Reference

Interplay between metal binding and cis/trans isomerization in legume lectins: structural and thermodynamic study of P. angolensis lectin., Garcia-Pino A, Buts L, Wyns L, Loris R, J Mol Biol. 2006 Aug 4;361(1):153-67. Epub 2006 Jun 21. PMID:16824540

Page seeded by OCA on Tue Jan 29 20:03:18 2008

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