2gnt: Difference between revisions

Revision as of 18:33, 21 February 2008

EDTA treated P. angolensis lectin (PAL) remetallized with calcium (1 hour treatment)

OverviewOverview

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 StructureAbout this Structure

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

ReferenceReference

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 17:33:32 2008

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OCA

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 ==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.
+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==
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 [[Category: remetallization]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 20:04:15 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:33:32 2008''