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Interplay between metal binding and cis/trans isomerization in legume lectins: structural and thermodynamic study of P. angolensis lectin.

Abstract：

: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.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Garcia-Pino A,Buts L,Wyns L,Loris R

doi

10.1016/j.jmb.2006.06.006

subject

Has Abstract

pub_date

2006-08-04 00:00:00

pages

153-67

issue

1

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(06)00698-X

journal_volume

361

pub_type

杂志文章

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