2GNT: Edta Treated P. Angolensis Lectin (pal) Remetallized With Calcium (1 Hour Treatment)

Citation:
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.
PDB ID: 2GNTDownload
MMDB ID: 40467
PDB Deposition Date: 2006/4/11
Updated in MMDB: 2017/10
Experimental Method:
x-ray diffraction
Resolution: 2.02  Å
Source Organism:
Similar Structures:
Biological Unit for 2GNT: dimeric; determined by author and by software (PISA)
Molecular Components in 2GNT
Label Count Molecule
Proteins (2 molecules)
2
Lectin
Molecule annotation
Chemicals (4 molecules)
1
4
* Click molecule labels to explore molecular sequence information.

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