2GNT

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

Summary for 2GNT

• Entry DOI: 10.2210/pdb2gnt/pdb
• Related: 1UKG 2GME 2GMM 2GMP 2GN3 2GNB 2GND 2GNM
• Descriptor: lectin, CALCIUM ION (3 entities in total)
• Functional Keywords: legume lectin, remetallization, pal, metal binding, beta sandwich, sugar binding protein
• Biological source: Pterocarpus angolensis
• Total number of polymer chains: 2
• Total formula weight: 55276.91

Authors

Garcia-Pino, A.,Buts, L.,Wyns, L.,Loris, R. (deposition date: 2006-04-11, release date: 2006-07-25, Last modification date: 2024-10-09)

Primary citation

Garcia-Pino, A.,Buts, L.,Wyns, L.,Loris, R.
Interplay Between Metal Binding and cis/trans Isomerization in Legume Lectins: Structural and Thermodynamic Study of P. angolensis Lectin.
J.Mol.Biol., 361:153-167, 2006

PubMed 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.

PubMed: 16824540
DOI: 10.1016/j.jmb.2006.06.006

Experimental method

X-RAY DIFFRACTION (2.02 Å)