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

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: 2GMMDownload
MMDB ID: 40459
PDB Deposition Date: 2006/4/7
Updated in MMDB: 2017/10
Experimental Method:
x-ray diffraction
Resolution: 2.15  Å
Source Organism:
Similar Structures:
Biological Unit for 2GMM: dimeric; determined by author and by software (PISA)
Molecular Components in 2GMM
Label Count Molecule
Proteins (2 molecules)
2
Lectin
Molecule annotation
Chemicals (6 molecules)
1
4
2
2
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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