2gmm
From Proteopedia
(New page: 200px<br /><applet load="2gmm" size="350" color="white" frame="true" align="right" spinBox="true" caption="2gmm, resolution 2.15Å" /> '''Metal-free (apo) P. ...) |
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==Overview== | ==Overview== | ||
| - | The interplay between metal binding, carbohydrate binding activity, stability and structure of the lectin from Pterocarpus angolensis was | + | 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== | ==About this Structure== | ||
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[[Category: sugar complex]] | [[Category: sugar complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:33:11 2008'' |
Revision as of 15:33, 21 February 2008
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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 Thu Feb 21 17:33:11 2008
